PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 30770797-3 2019 The complex includes the heat-shock chaperonin pair, HSP60/10, which is likely involved in importing Fhit into the mitochondria, where it interacts with ferredoxin reductase, responsible for transferring electrons from NADPH to cytochrome P450 via ferredoxin, in electron transport chain complex III. NADP 219-224 ferredoxin reductase Homo sapiens 153-173 30633837-2 2019 In a chemical analogue exploiting this principle, nicotinamide adenine dinucleotide phosphate (NADPH) and NADP+ are cycled rapidly between ferredoxin-NADP+ reductase and a second enzyme-the pairs being juxtaposed within the 5-100 nm scale pores of an indium tin oxide electrode. NADP 50-93 ferredoxin reductase Homo sapiens 139-165 30633837-2 2019 In a chemical analogue exploiting this principle, nicotinamide adenine dinucleotide phosphate (NADPH) and NADP+ are cycled rapidly between ferredoxin-NADP+ reductase and a second enzyme-the pairs being juxtaposed within the 5-100 nm scale pores of an indium tin oxide electrode. NADP 95-100 ferredoxin reductase Homo sapiens 139-165 30633837-2 2019 In a chemical analogue exploiting this principle, nicotinamide adenine dinucleotide phosphate (NADPH) and NADP+ are cycled rapidly between ferredoxin-NADP+ reductase and a second enzyme-the pairs being juxtaposed within the 5-100 nm scale pores of an indium tin oxide electrode. NADP 106-111 ferredoxin reductase Homo sapiens 139-165 29040572-3 2017 Here, we conducted whole-exome sequencing of patients with optic atrophy and other neurological signs of mitochondriopathy and identified 17 individuals from 13 unrelated families with recessive mutations in FDXR, encoding the mitochondrial membrane-associated flavoprotein ferrodoxin reductase required for electron transport from NADPH to cytochrome P450. NADP 332-337 ferredoxin reductase Homo sapiens 208-212 29177972-0 2017 Conservation of the Enzyme-Coenzyme Interfaces in FAD and NADP Binding Adrenodoxin Reductase-A Ubiquitous Enzyme. NADP 58-62 ferredoxin reductase Homo sapiens 71-92 29177972-7 2017 The NADP binding site of all AdxR orthologs showed a modified Rossmann fold motif with a GxGxxA consensus instead of the classical GxGxxG at the edge of the first betaalpha-fold. NADP 4-8 ferredoxin reductase Homo sapiens 29-33 27049848-5 2016 We first used our approach to quantitatively characterize electron transfer from NADPH through Adrenodoxin Reductase (AdR) to Adrenodoxin (Adx). NADP 81-86 ferredoxin reductase Homo sapiens 95-116 30155220-1 2017 In a discovery of the transfer of chloroplast biosynthesis activity to an inorganic material, ferredoxin-NADP+ reductase (FNR), the pivotal redox flavoenzyme of photosynthetic CO2 assimilation, binds tightly within the pores of indium tin oxide (ITO) to produce an electrode for direct studies of the redox chemistry of the FAD active site, and fast, reversible and diffusion-controlled interconversion of NADP+ and NADPH in solution. NADP 105-110 ferredoxin reductase Homo sapiens 122-125 30155220-1 2017 In a discovery of the transfer of chloroplast biosynthesis activity to an inorganic material, ferredoxin-NADP+ reductase (FNR), the pivotal redox flavoenzyme of photosynthetic CO2 assimilation, binds tightly within the pores of indium tin oxide (ITO) to produce an electrode for direct studies of the redox chemistry of the FAD active site, and fast, reversible and diffusion-controlled interconversion of NADP+ and NADPH in solution. NADP 416-421 ferredoxin reductase Homo sapiens 94-120 30155220-1 2017 In a discovery of the transfer of chloroplast biosynthesis activity to an inorganic material, ferredoxin-NADP+ reductase (FNR), the pivotal redox flavoenzyme of photosynthetic CO2 assimilation, binds tightly within the pores of indium tin oxide (ITO) to produce an electrode for direct studies of the redox chemistry of the FAD active site, and fast, reversible and diffusion-controlled interconversion of NADP+ and NADPH in solution. NADP 416-421 ferredoxin reductase Homo sapiens 122-125 31968797-2 2016 The activity of P450scc is dependent upon electron delivery from NADPH-dependent adrenodoxin reductase (AdR), via adrenodoxin (Adx), to the P450scc. NADP 65-70 ferredoxin reductase Homo sapiens 81-102 31968797-2 2016 The activity of P450scc is dependent upon electron delivery from NADPH-dependent adrenodoxin reductase (AdR), via adrenodoxin (Adx), to the P450scc. NADP 65-70 ferredoxin reductase Homo sapiens 104-107 27049848-5 2016 We first used our approach to quantitatively characterize electron transfer from NADPH through Adrenodoxin Reductase (AdR) to Adrenodoxin (Adx). NADP 81-86 ferredoxin reductase Homo sapiens 118-121 25209177-4 2015 The first author (PKM) personally acted as Ferredoxin NADP Reductase (FNR) catalyzing the reduction of NADP(+) to NADPH, taking electrons from reduced ferredoxin at the end of Photosystem I. NADP 103-110 ferredoxin reductase Homo sapiens 43-68 26248023-1 2015 The complexes formed between the flavoenzyme ferredoxin-NADP(+) reductase (FNR; NADP(+) =nicotinamide adenine dinucleotide phosphate) and its redox protein partners, ferredoxin (Fd) and flavodoxin (Fld), have been analysed by using dynamic force spectroscopy through AFM. NADP 56-63 ferredoxin reductase Homo sapiens 75-78 26248023-1 2015 The complexes formed between the flavoenzyme ferredoxin-NADP(+) reductase (FNR; NADP(+) =nicotinamide adenine dinucleotide phosphate) and its redox protein partners, ferredoxin (Fd) and flavodoxin (Fld), have been analysed by using dynamic force spectroscopy through AFM. NADP 89-132 ferredoxin reductase Homo sapiens 45-73 26248023-1 2015 The complexes formed between the flavoenzyme ferredoxin-NADP(+) reductase (FNR; NADP(+) =nicotinamide adenine dinucleotide phosphate) and its redox protein partners, ferredoxin (Fd) and flavodoxin (Fld), have been analysed by using dynamic force spectroscopy through AFM. NADP 89-132 ferredoxin reductase Homo sapiens 75-78 25209177-4 2015 The first author (PKM) personally acted as Ferredoxin NADP Reductase (FNR) catalyzing the reduction of NADP(+) to NADPH, taking electrons from reduced ferredoxin at the end of Photosystem I. NADP 114-119 ferredoxin reductase Homo sapiens 43-68 20453296-1 2010 Ferredoxin reduced by Photosystem I in light serves as an electron donor for the reduction of NADP(+) to NADPH, and this reaction is catalyzed by enzyme ferredoxin:NADP(+)-reductase (FNR). NADP 94-101 ferredoxin reductase Homo sapiens 153-181 24321506-1 2014 Ferredoxin-NADP(+) reductase (FNR) is the structural prototype of a family of FAD-containing reductases that catalyze electron transfer between low potential proteins and NAD(P)(+)/H, and that display a two-domain arrangement with an open cavity at their interface. NADP 171-180 ferredoxin reductase Homo sapiens 0-28 24321506-1 2014 Ferredoxin-NADP(+) reductase (FNR) is the structural prototype of a family of FAD-containing reductases that catalyze electron transfer between low potential proteins and NAD(P)(+)/H, and that display a two-domain arrangement with an open cavity at their interface. NADP 171-180 ferredoxin reductase Homo sapiens 30-33 23289611-2 2013 Evidence suggests that the FMN-binding domain undergoes large conformational motions to shuttle electrons between the NADPH/FAD-binding domain [FNR (ferredoxin NADP-reductase)] and the oxygenase domain. NADP 118-123 ferredoxin reductase Homo sapiens 149-174 23181670-1 2012 During photosynthesis, ferredoxin-NADP(+) reductase (FNR) catalyzes the electron transfer from ferredoxin to NADP(+) via its FAD cofactor. NADP 34-38 ferredoxin reductase Homo sapiens 53-56 23181670-3 2012 Two different transient charge-transfer complexes form prior to and upon hydride transfer, FNR(rd)-NADP(+) and FNR(ox)-NADPH, regardless of the hydride transfer direction. NADP 99-103 ferredoxin reductase Homo sapiens 91-94 23181670-3 2012 Two different transient charge-transfer complexes form prior to and upon hydride transfer, FNR(rd)-NADP(+) and FNR(ox)-NADPH, regardless of the hydride transfer direction. NADP 119-124 ferredoxin reductase Homo sapiens 111-114 23181670-4 2012 Experimental structures of the FNR(ox):NADP(+) interaction have suggested a series of conformational rearrangements that might contribute to attaining the catalytically competent complex, but to date, no direct experimental information about the structure of this complex is available. NADP 39-46 ferredoxin reductase Homo sapiens 31-34 23181670-5 2012 Recently, a molecular dynamics (MD) theoretical approach was used to provide a putative organization of the active site that might represent a structure close to the transient catalytically competent interaction of Anabaena FNR with its coenzyme, NADP(+). NADP 249-253 ferredoxin reductase Homo sapiens 226-229 22542899-1 2012 The role of the highly conserved C266 and L268 of pea ferredoxin-NADP(+) reductase (FNR) in formation of the catalytically competent complex of the enzyme with NADP(H) was investigated. NADP 160-167 ferredoxin reductase Homo sapiens 54-82 22542899-1 2012 The role of the highly conserved C266 and L268 of pea ferredoxin-NADP(+) reductase (FNR) in formation of the catalytically competent complex of the enzyme with NADP(H) was investigated. NADP 160-167 ferredoxin reductase Homo sapiens 84-87 22542899-10 2012 In addition, flexibility of the 268-270 loop appears to be critical for FNR to achieve catalytically competent complexes with NADP(H). NADP 126-133 ferredoxin reductase Homo sapiens 72-75 21538059-1 2012 Ferredoxin-NADP(+) reductase (FNR) catalyses the electron transfer from ferredoxin to NADP(+) via its flavin FAD cofactor. NADP 11-18 ferredoxin reductase Homo sapiens 30-33 21538059-2 2012 A molecular dynamics theoretical approach is applied here to visualise the transient catalytically competent interaction of Anabaena FNR with its coenzyme, NADP(+). NADP 156-163 ferredoxin reductase Homo sapiens 133-136 24402199-1 2014 Ferredoxin-NADP+ reductase (FNR) catalyzes the electron transfer from ferredoxin to NADP+ via its flavin FAD cofactor. NADP 11-16 ferredoxin reductase Homo sapiens 28-31 24321386-1 2014 Ferredoxin reductase (FDXR, also known as adrenodoxin reductase) is a mitochondrial flavoprotein that transfers electrons from NADPH to mitochondrial cytochrome P450 enzymes, mediating the function of an iron-sulfur cluster protein, ferredoxin. NADP 127-132 ferredoxin reductase Homo sapiens 0-20 24321386-1 2014 Ferredoxin reductase (FDXR, also known as adrenodoxin reductase) is a mitochondrial flavoprotein that transfers electrons from NADPH to mitochondrial cytochrome P450 enzymes, mediating the function of an iron-sulfur cluster protein, ferredoxin. NADP 127-132 ferredoxin reductase Homo sapiens 22-26 24321386-1 2014 Ferredoxin reductase (FDXR, also known as adrenodoxin reductase) is a mitochondrial flavoprotein that transfers electrons from NADPH to mitochondrial cytochrome P450 enzymes, mediating the function of an iron-sulfur cluster protein, ferredoxin. NADP 127-132 ferredoxin reductase Homo sapiens 42-63 23618857-1 2013 Ferredoxin-NADP(+) reductase (FNR) forms a 1:1 complex with ferredoxin (Fd), and catalyzes the electron transfer between Fd and NADP(+). NADP 11-15 ferredoxin reductase Homo sapiens 30-33 21526428-2 2011 The reduction equivalents for this reaction are provided by NADPH, via a small electron transfer chain, consisting of adrenodoxin reductase (AdR) and adrenodoxin (Adx). NADP 60-65 ferredoxin reductase Homo sapiens 118-139 21526428-2 2011 The reduction equivalents for this reaction are provided by NADPH, via a small electron transfer chain, consisting of adrenodoxin reductase (AdR) and adrenodoxin (Adx). NADP 60-65 ferredoxin reductase Homo sapiens 141-144 20471952-1 2010 Two transient charge-transfer complexes (CTC) form prior and upon hydride transfer (HT) in the reversible reaction of the FAD-dependent ferredoxin-NADP+ reductase (FNR) with NADP+/H, FNR(ox)-NADPH (CTC-1), and FNR(rd)-NADP+ (CTC-2). NADP 147-151 ferredoxin reductase Homo sapiens 164-167 20471952-1 2010 Two transient charge-transfer complexes (CTC) form prior and upon hydride transfer (HT) in the reversible reaction of the FAD-dependent ferredoxin-NADP+ reductase (FNR) with NADP+/H, FNR(ox)-NADPH (CTC-1), and FNR(rd)-NADP+ (CTC-2). NADP 147-151 ferredoxin reductase Homo sapiens 183-186 20471952-1 2010 Two transient charge-transfer complexes (CTC) form prior and upon hydride transfer (HT) in the reversible reaction of the FAD-dependent ferredoxin-NADP+ reductase (FNR) with NADP+/H, FNR(ox)-NADPH (CTC-1), and FNR(rd)-NADP+ (CTC-2). NADP 147-151 ferredoxin reductase Homo sapiens 183-186 20471952-1 2010 Two transient charge-transfer complexes (CTC) form prior and upon hydride transfer (HT) in the reversible reaction of the FAD-dependent ferredoxin-NADP+ reductase (FNR) with NADP+/H, FNR(ox)-NADPH (CTC-1), and FNR(rd)-NADP+ (CTC-2). NADP 191-196 ferredoxin reductase Homo sapiens 136-162 20471952-1 2010 Two transient charge-transfer complexes (CTC) form prior and upon hydride transfer (HT) in the reversible reaction of the FAD-dependent ferredoxin-NADP+ reductase (FNR) with NADP+/H, FNR(ox)-NADPH (CTC-1), and FNR(rd)-NADP+ (CTC-2). NADP 191-196 ferredoxin reductase Homo sapiens 164-167 20471952-1 2010 Two transient charge-transfer complexes (CTC) form prior and upon hydride transfer (HT) in the reversible reaction of the FAD-dependent ferredoxin-NADP+ reductase (FNR) with NADP+/H, FNR(ox)-NADPH (CTC-1), and FNR(rd)-NADP+ (CTC-2). NADP 191-196 ferredoxin reductase Homo sapiens 183-186 20471952-1 2010 Two transient charge-transfer complexes (CTC) form prior and upon hydride transfer (HT) in the reversible reaction of the FAD-dependent ferredoxin-NADP+ reductase (FNR) with NADP+/H, FNR(ox)-NADPH (CTC-1), and FNR(rd)-NADP+ (CTC-2). NADP 191-196 ferredoxin reductase Homo sapiens 183-186 20471952-1 2010 Two transient charge-transfer complexes (CTC) form prior and upon hydride transfer (HT) in the reversible reaction of the FAD-dependent ferredoxin-NADP+ reductase (FNR) with NADP+/H, FNR(ox)-NADPH (CTC-1), and FNR(rd)-NADP+ (CTC-2). NADP 174-178 ferredoxin reductase Homo sapiens 136-162 20471952-1 2010 Two transient charge-transfer complexes (CTC) form prior and upon hydride transfer (HT) in the reversible reaction of the FAD-dependent ferredoxin-NADP+ reductase (FNR) with NADP+/H, FNR(ox)-NADPH (CTC-1), and FNR(rd)-NADP+ (CTC-2). NADP 174-178 ferredoxin reductase Homo sapiens 164-167 20471952-1 2010 Two transient charge-transfer complexes (CTC) form prior and upon hydride transfer (HT) in the reversible reaction of the FAD-dependent ferredoxin-NADP+ reductase (FNR) with NADP+/H, FNR(ox)-NADPH (CTC-1), and FNR(rd)-NADP+ (CTC-2). NADP 174-178 ferredoxin reductase Homo sapiens 183-186 20471952-1 2010 Two transient charge-transfer complexes (CTC) form prior and upon hydride transfer (HT) in the reversible reaction of the FAD-dependent ferredoxin-NADP+ reductase (FNR) with NADP+/H, FNR(ox)-NADPH (CTC-1), and FNR(rd)-NADP+ (CTC-2). NADP 174-178 ferredoxin reductase Homo sapiens 183-186 20407804-3 2010 The second enzyme that requires NADPH as an electron donor was a 30 kDa protein, and N-terminal sequencing revealed it to be ferredoxin-NADP(+) reductase (Fpr). NADP 32-37 ferredoxin reductase Homo sapiens 125-153 20407804-3 2010 The second enzyme that requires NADPH as an electron donor was a 30 kDa protein, and N-terminal sequencing revealed it to be ferredoxin-NADP(+) reductase (Fpr). NADP 32-37 ferredoxin reductase Homo sapiens 155-158 20163096-2 2010 The flavoenzyme ferredoxin-NADP(+) reductase (FNR) catalyzes the production of NADPH during photosynthesis. NADP 79-84 ferredoxin reductase Homo sapiens 16-44 20163096-2 2010 The flavoenzyme ferredoxin-NADP(+) reductase (FNR) catalyzes the production of NADPH during photosynthesis. NADP 79-84 ferredoxin reductase Homo sapiens 46-49 20453296-1 2010 Ferredoxin reduced by Photosystem I in light serves as an electron donor for the reduction of NADP(+) to NADPH, and this reaction is catalyzed by enzyme ferredoxin:NADP(+)-reductase (FNR). NADP 94-101 ferredoxin reductase Homo sapiens 183-186 20453296-1 2010 Ferredoxin reduced by Photosystem I in light serves as an electron donor for the reduction of NADP(+) to NADPH, and this reaction is catalyzed by enzyme ferredoxin:NADP(+)-reductase (FNR). NADP 105-110 ferredoxin reductase Homo sapiens 153-181 20453296-1 2010 Ferredoxin reduced by Photosystem I in light serves as an electron donor for the reduction of NADP(+) to NADPH, and this reaction is catalyzed by enzyme ferredoxin:NADP(+)-reductase (FNR). NADP 105-110 ferredoxin reductase Homo sapiens 183-186 16216071-0 2005 C-terminal tyrosine of ferredoxin-NADP+ reductase in hydride transfer processes with NAD(P)+/H. NADP 85-92 ferredoxin reductase Homo sapiens 23-49 16289098-3 2005 In this study, LytB of P. falciparum was shown to be catalytically active in the presence of an NADPH dependent electron transfer system comprising ferredoxin and ferredoxin-NADP(+) reductase. NADP 96-101 ferredoxin reductase Homo sapiens 163-191 19583765-1 2009 This minireview covers the research carried out in recent years into different aspects of the function of the flavoproteins involved in cyanobacterial photosynthetic electron transfer from photosystem I to NADP(+), flavodoxin and ferredoxin-NADP(+) reductase. NADP 206-210 ferredoxin reductase Homo sapiens 230-258 18260112-1 2008 Ferredoxin (Fd) interacts with ferredoxin-NADP(+) reductase (FNR) to transfer two electrons to the latter, one by one, which will finally be used to reduce NADP(+) to NADPH. NADP 42-49 ferredoxin reductase Homo sapiens 61-64 18260112-1 2008 Ferredoxin (Fd) interacts with ferredoxin-NADP(+) reductase (FNR) to transfer two electrons to the latter, one by one, which will finally be used to reduce NADP(+) to NADPH. NADP 167-172 ferredoxin reductase Homo sapiens 31-59 18260112-1 2008 Ferredoxin (Fd) interacts with ferredoxin-NADP(+) reductase (FNR) to transfer two electrons to the latter, one by one, which will finally be used to reduce NADP(+) to NADPH. NADP 167-172 ferredoxin reductase Homo sapiens 61-64 18319262-3 2008 The complex includes Hsp60 and Hsp10 that mediate Fhit stability and may affect import into mitochondria, where it interacts with ferredoxin reductase, responsible for transferring electrons from NADPH to cytochrome P450 via ferredoxin. NADP 196-201 ferredoxin reductase Homo sapiens 130-150 17635583-0 2007 Enzymatic oxidation of NADP+ to its 4-oxo derivative is a side-reaction displayed only by the adrenodoxin reductase type of ferredoxin-NADP+ reductases. NADP 23-27 ferredoxin reductase Homo sapiens 94-115 17635583-6 2007 Whereas plant-type ferredoxin reductases were unable to oxidize NADP(+), the mammalian adrenodoxin reductase also catalyzed this unusual reaction. NADP 64-68 ferredoxin reductase Homo sapiens 87-108 16762315-3 2006 In the linear mode, Fd binds ferredoxin-NADP-reductase and electrons are transferred to NADP+ and then to the Benson and Calvin cycle. NADP 88-93 ferredoxin reductase Homo sapiens 29-54 16216071-1 2005 Ferredoxin-NADP+ reductase (FNR) catalyzes the reduction of NADP+ to NADPH in an overall reversible reaction, showing some differences in the mechanisms between cyanobacterial and higher plant FNRs. NADP 11-16 ferredoxin reductase Homo sapiens 28-31 16216071-1 2005 Ferredoxin-NADP+ reductase (FNR) catalyzes the reduction of NADP+ to NADPH in an overall reversible reaction, showing some differences in the mechanisms between cyanobacterial and higher plant FNRs. NADP 69-74 ferredoxin reductase Homo sapiens 0-26 16216071-1 2005 Ferredoxin-NADP+ reductase (FNR) catalyzes the reduction of NADP+ to NADPH in an overall reversible reaction, showing some differences in the mechanisms between cyanobacterial and higher plant FNRs. NADP 69-74 ferredoxin reductase Homo sapiens 28-31 16216071-5 2005 All FNR variants show enhanced NADP+ and NAD+ binding, especially Tyr303Ser, which correlates with a noticeable improvement of NADH-dependent reactions. NADP 31-36 ferredoxin reductase Homo sapiens 4-7 16216071-10 2005 Additionally, it is shown that the C-terminal Tyr of FNR lowers the affinity for NADP+/H to levels compatible with steady-state turnover during the catalytic cycle, but it is not involved in the hydride transfer itself. NADP 81-85 ferredoxin reductase Homo sapiens 53-56 12383252-1 2002 The role of the negative charge of the E139 side-chain of Anabaena Ferredoxin-NADP+ reductase (FNR) in steering appropriate docking with its substrates ferredoxin, flavodoxin and NADP+/H, that leads to efficient electron transfer (ET) is analysed by characterization of several E139 FNR mutants. NADP 78-82 ferredoxin reductase Homo sapiens 95-98 16087182-0 2005 Synechocystis ferredoxin/ferredoxin-NADP(+)-reductase/NADP+ complex: Structural model obtained by NMR-restrained docking. NADP 54-59 ferredoxin reductase Homo sapiens 25-53 16087182-2 2005 Based on a nuclear magnetic resonance (NMR)-restrained-docking approach, two alternative structural models of the Fd-FNR complex in the presence of NADP+ are proposed. NADP 148-153 ferredoxin reductase Homo sapiens 117-120 16328828-3 2004 Because the reaction mechanism of ferredoxin-NADP reducing system was clarified in the isolated enzyme system, it was generally thought that the role of FNR in the NADP photoreduction of chloroplasts had been fully elucidated. NADP 45-49 ferredoxin reductase Homo sapiens 153-156 16328828-3 2004 Because the reaction mechanism of ferredoxin-NADP reducing system was clarified in the isolated enzyme system, it was generally thought that the role of FNR in the NADP photoreduction of chloroplasts had been fully elucidated. NADP 164-168 ferredoxin reductase Homo sapiens 153-156 16328828-4 2004 However, the results of a reconstitution study using the crystallized FNR and the depleted grana, from which "built-in" FNR had been eliminated, showed that the NADP photoreducing activity of reconstituted FNR was much lower than the original physiological activity, and as a result, more studies had to be continued. NADP 161-165 ferredoxin reductase Homo sapiens 70-73 16328828-4 2004 However, the results of a reconstitution study using the crystallized FNR and the depleted grana, from which "built-in" FNR had been eliminated, showed that the NADP photoreducing activity of reconstituted FNR was much lower than the original physiological activity, and as a result, more studies had to be continued. NADP 161-165 ferredoxin reductase Homo sapiens 120-123 16328828-4 2004 However, the results of a reconstitution study using the crystallized FNR and the depleted grana, from which "built-in" FNR had been eliminated, showed that the NADP photoreducing activity of reconstituted FNR was much lower than the original physiological activity, and as a result, more studies had to be continued. NADP 161-165 ferredoxin reductase Homo sapiens 120-123 16328828-6 2004 Then in 1991, the FNR-connectein complex was formed using purified connectein and FNR, and after eliminating "built-in" FNR, the reconstituted complex was bound to the depleted grana having reduced NADP photoreducing activity. NADP 198-202 ferredoxin reductase Homo sapiens 18-21 16328828-8 2004 This proved that the FNR-connectein complex, which binds to a specific site on the surface of thylakoid membrane, is functionally responsible for NADP photoreduction in chloroplasts. NADP 146-150 ferredoxin reductase Homo sapiens 21-24 14529296-3 2003 Similar quenching was also observed with the addition of heparin or thenoyltrifluoroacetone (TTFA), inhibitors that bind ferredoxin:NADP(+) reductase (FNR) and prevent reduction of NADP(+). NADP 132-136 ferredoxin reductase Homo sapiens 151-154 14529296-7 2003 Conformational modification of FNR upon binding of NADP(+) or NADPH is proposed to trigger the macromolecular changes in a larger part of the protein complex of PSI. NADP 51-58 ferredoxin reductase Homo sapiens 31-34 14529296-7 2003 Conformational modification of FNR upon binding of NADP(+) or NADPH is proposed to trigger the macromolecular changes in a larger part of the protein complex of PSI. NADP 62-67 ferredoxin reductase Homo sapiens 31-34 12370809-2 2002 Ferredoxin Reductase (protein, FR; gene, FDXR) transfers electron from NADPH to cytochrome P450 via ferredoxin in mitochondria. NADP 71-76 ferredoxin reductase Homo sapiens 0-20 12370809-2 2002 Ferredoxin Reductase (protein, FR; gene, FDXR) transfers electron from NADPH to cytochrome P450 via ferredoxin in mitochondria. NADP 71-76 ferredoxin reductase Homo sapiens 41-45 12359874-1 2002 Nitric oxide synthases (NOSs) are flavoheme enzymes that contain a ferredoxin:NADP(+)-reductase (FNR) module for binding NADPH and FAD and are unusual because their electron transfer reactions are controlled by the Ca(2+)-binding protein calmodulin. NADP 121-126 ferredoxin reductase Homo sapiens 67-95 12359874-1 2002 Nitric oxide synthases (NOSs) are flavoheme enzymes that contain a ferredoxin:NADP(+)-reductase (FNR) module for binding NADPH and FAD and are unusual because their electron transfer reactions are controlled by the Ca(2+)-binding protein calmodulin. NADP 121-126 ferredoxin reductase Homo sapiens 97-100 12359874-2 2002 A conserved aromatic residue in the FNR module of NOS shields the isoalloxazine ring of FAD and is known to regulate NADPH binding affinity and specificity in related flavoproteins. NADP 117-122 ferredoxin reductase Homo sapiens 36-39 14966111-2 2004 The NOS flavoprotein domain includes a ferredoxin-NADP(+) reductase (FNR)-like module that contains NADPH- and FAD-binding sites. NADP 100-105 ferredoxin reductase Homo sapiens 39-67 14966111-2 2004 The NOS flavoprotein domain includes a ferredoxin-NADP(+) reductase (FNR)-like module that contains NADPH- and FAD-binding sites. NADP 100-105 ferredoxin reductase Homo sapiens 69-72 16228387-4 2004 In this system the enzyme responsible for NADP(+) reduction is ferredoxin-NADP(+) reductase (FNR), a FAD-containing NADP(+) dependent reductase. NADP 42-49 ferredoxin reductase Homo sapiens 63-91 16228387-4 2004 In this system the enzyme responsible for NADP(+) reduction is ferredoxin-NADP(+) reductase (FNR), a FAD-containing NADP(+) dependent reductase. NADP 42-49 ferredoxin reductase Homo sapiens 93-96 16228387-7 2004 The processes of interaction and ET between FNR and all of its substrates involved in the photosynthetic ET chain, namely Fd, Fld and NADP(+)/H have been extensively investigated in recent years using a large number of techniques, including the introduction of site-specific mutations in combination with kinetic and structural studies of the produced mutants. NADP 134-138 ferredoxin reductase Homo sapiens 44-47 16034533-1 2004 The plant-type ferredoxins (Fds) are the [2Fe-2S] proteins that function primarily in photosynthesis; they transfer electrons from photoreduced Photosystem I to ferredoxin NADP(+) reductase in which NADPH is produced for CO(2) assimilation. NADP 199-204 ferredoxin reductase Homo sapiens 161-189 16034534-1 2004 Ferredoxin reductase (FNR) is ubiquitous among photosynthetic organisms as the enzyme directly responsible for the generation of NADPH. NADP 129-134 ferredoxin reductase Homo sapiens 0-20 16034534-1 2004 Ferredoxin reductase (FNR) is ubiquitous among photosynthetic organisms as the enzyme directly responsible for the generation of NADPH. NADP 129-134 ferredoxin reductase Homo sapiens 22-25 14657394-5 2003 In this article, we describe in vitro experiments using purified mitochondrial cytochrome P450scc (CYP11A1) reconstituted with the iron-sulfer protein, adrenodoxin, and the flavoprotein, adrenodoxin reductase, and show the NADPH and time-dependent formation of two major metabolites of D3 (i.e., 20-hydroxyvitamin D3 and 20,22-dihydroxyvitamin D3) plus two unknown minor metabolites. NADP 223-228 ferredoxin reductase Homo sapiens 187-208 12383252-1 2002 The role of the negative charge of the E139 side-chain of Anabaena Ferredoxin-NADP+ reductase (FNR) in steering appropriate docking with its substrates ferredoxin, flavodoxin and NADP+/H, that leads to efficient electron transfer (ET) is analysed by characterization of several E139 FNR mutants. NADP 78-82 ferredoxin reductase Homo sapiens 283-286 11298752-3 2001 Adrenodoxin reductase serves to reduce adrenodoxin as part of the electron transfer from NADPH to cytochrome P450scc. NADP 89-94 ferredoxin reductase Homo sapiens 0-21 12079352-1 2002 The flavoenzyme ferredoxin-NADP+ reductase (FNR) catalyses the production of NADPH in photosynthesis. NADP 77-82 ferredoxin reductase Homo sapiens 16-42 12079352-1 2002 The flavoenzyme ferredoxin-NADP+ reductase (FNR) catalyses the production of NADPH in photosynthesis. NADP 77-82 ferredoxin reductase Homo sapiens 44-47 12079352-2 2002 The three-dimensional structure of FNR presents two distinct domains, one for binding of the FAD prosthetic group and the other for NADP+ binding. NADP 132-137 ferredoxin reductase Homo sapiens 35-38 12079352-3 2002 In spite of extensive experiments and different crystallographic approaches, many aspects about how the NADP+ substrate binds to FNR and how the hydride ion is transferred from FAD to NADP+ remain unclear. NADP 104-109 ferredoxin reductase Homo sapiens 129-132 12079352-4 2002 The structure of an FNR:NADP+ complex from Anabaena has been determined by X-ray diffraction analysis of the cocrystallised units to 2.1 A resolution. NADP 24-29 ferredoxin reductase Homo sapiens 20-23 12079352-5 2002 Structural perturbation of FNR induced by complex formation produces a narrower cavity in which the 2"-phospho-AMP and pyrophosphate portions of the NADP+ are perfectly bound. NADP 149-154 ferredoxin reductase Homo sapiens 27-30 12079352-7 2002 The crystal structure of this FNR:NADP+ complex obtained by cocrystallisation displays NADP+ in an unusual conformation and can be considered as an intermediate state in the process of coenzyme recognition and binding. NADP 34-39 ferredoxin reductase Homo sapiens 30-33 12079352-7 2002 The crystal structure of this FNR:NADP+ complex obtained by cocrystallisation displays NADP+ in an unusual conformation and can be considered as an intermediate state in the process of coenzyme recognition and binding. NADP 87-92 ferredoxin reductase Homo sapiens 30-33 12079352-9 2002 Besides, this structure gives new insights into the postulated formation of the ferredoxin:FNR:NADP+ ternary complex by prediction of new intermolecular interactions, which could only exist after FNR:NADP+ complex formation. NADP 95-100 ferredoxin reductase Homo sapiens 91-94 12079352-9 2002 Besides, this structure gives new insights into the postulated formation of the ferredoxin:FNR:NADP+ ternary complex by prediction of new intermolecular interactions, which could only exist after FNR:NADP+ complex formation. NADP 95-100 ferredoxin reductase Homo sapiens 196-199 12079352-9 2002 Besides, this structure gives new insights into the postulated formation of the ferredoxin:FNR:NADP+ ternary complex by prediction of new intermolecular interactions, which could only exist after FNR:NADP+ complex formation. NADP 200-205 ferredoxin reductase Homo sapiens 91-94 12079352-9 2002 Besides, this structure gives new insights into the postulated formation of the ferredoxin:FNR:NADP+ ternary complex by prediction of new intermolecular interactions, which could only exist after FNR:NADP+ complex formation. NADP 200-205 ferredoxin reductase Homo sapiens 196-199 12079352-10 2002 Finally, structural comparison with the members of the broad FNR structural family also provides an explanation for the high specificity exhibited by FNR for NADP+/H versus NAD+/H. NADP 158-163 ferredoxin reductase Homo sapiens 61-64 12079352-10 2002 Finally, structural comparison with the members of the broad FNR structural family also provides an explanation for the high specificity exhibited by FNR for NADP+/H versus NAD+/H. NADP 158-163 ferredoxin reductase Homo sapiens 150-153 12009436-1 2002 The enzyme Ferredoxin-NADP(+) reductase participates in the reductive side of the photosynthetic chain transferring electrons from reduced Ferredoxin (Fd) (or Flavodoxin (Fld)) to NADP(+), a process that yields NADPH that can be used in many biosynthetic dark reactions. NADP 211-216 ferredoxin reductase Homo sapiens 11-39 11256611-2 2000 FNR uses two high energy electrons photoproduced by photosystem I (PSI) and conveyed, one by one, by a ferredoxin (Fd), to reduce NADP+ to NADPH. NADP 130-135 ferredoxin reductase Homo sapiens 0-3 11400110-3 2001 It also catalyzed the photoreduction of NADP+ or NAD+ in the presence of ascorbate as an electron donor and ferredoxin-NADP+ reductase as the coupling enzyme. NADP 40-45 ferredoxin reductase Homo sapiens 108-134 11256611-2 2000 FNR uses two high energy electrons photoproduced by photosystem I (PSI) and conveyed, one by one, by a ferredoxin (Fd), to reduce NADP+ to NADPH. NADP 139-144 ferredoxin reductase Homo sapiens 0-3 10639079-4 2000 Furthermore, the PEG-chlorophyllin conjugate catalyzed the photoreduction of NADP(+) or NAD(+) in the presence of ascorbate as an electron donor and ferredoxin-NADP(+) reductase as the coupling enzyme. NADP 77-84 ferredoxin reductase Homo sapiens 149-177 10744737-1 2000 Chloroplast ferredoxin-NADP(+) reductase has a 32,000-fold preference for NADPH over NADH, consistent with its main physiological role of NADP(+) photoreduction for de novo carbohydrate biosynthesis. NADP 74-79 ferredoxin reductase Homo sapiens 12-40 10744737-6 2000 The data presented support the hypothesis that specific recognition of the 2"-phosphate group of NADP(H) is required but not sufficient to ensure a high degree of discrimination against NAD(H) in ferredoxin-NADP(+) reductase. NADP 97-104 ferredoxin reductase Homo sapiens 196-224 9893942-2 1998 This is the case for the flavoprotein ferredoxin:NADP+ reductase (FNR) from the cyanobacterium Anabaena, an enzyme which interacts with ferredoxin in the photosynthetic pathway to receive the electrons required for NADP+ reduction. NADP 49-54 ferredoxin reductase Homo sapiens 66-69 10550685-6 1999 The data presented here indicate that the mutated residues situated within the FNR FAD-binding domain are more important for achieving maximal ET rates, either with Fd or Fld, than those situated within the NADP(+)-binding domain, and that both ET proteins occupy the same region for the interaction with the reductase. NADP 207-214 ferredoxin reductase Homo sapiens 79-82 9511808-5 1998 Replacement of any one of these basic residues produced a much more pronounced effect on the cytochrome c reductase activity, where FNR, reduced by NADPH, acted as electron donor, than in the reduction of NADP+ by photosystem I via FNR. NADP 148-153 ferredoxin reductase Homo sapiens 132-135 9727014-3 1998 Adrenodoxin reductase transfers electrons from NADPH to adrenodoxin, which subsequently donates them to the cytochrome P450 forms. NADP 47-52 ferredoxin reductase Homo sapiens 0-21 9092820-2 1997 In this work, we show that the two flavin-based enzymes ferredoxin-NADP+ reductase and xanthine oxidase catalyze the reductive activation of 1 by NADPH and NADH, respectively. NADP 146-151 ferredoxin reductase Homo sapiens 56-82 1917982-1 1991 Ferredoxins found in animal mitochondria function in electron transfer from NADPH-dependent ferredoxin reductase (Fd-reductase) to cytochrome P450 enzymes. NADP 76-81 ferredoxin reductase Homo sapiens 92-112 8799343-4 1996 Anaerobic reduction of film incorporated cytochrome P450scc by electron transfer chain (NADPH-->adrenodoxin reductase-->adrenodoxin) revealed the low rate of the reaction that coincides well with the content of the hemoprotein low-spin form. NADP 88-93 ferredoxin reductase Homo sapiens 99-120 7677850-1 1995 The crystal structure of ferredoxin-NADP+ reductase (FNR) suggests that Ser96 is directly involved in hydride transfer between the isoalloxazine moiety of FAD and the nicotinamide ring of NADP(H). NADP 36-40 ferredoxin reductase Homo sapiens 53-56 7677850-6 1995 However, spectral perturbations induced by NADP+ binding to FNR-S96V strongly resemble those elicited by the binding of 2"-monophosphoadenosine-5"-diphosphoribose, a substrate analog lacking the nicotinamide ring, both to the mutant and wild-type enzymes. NADP 43-48 ferredoxin reductase Homo sapiens 60-63 7677850-12 1995 2% of the wild-type activity as well as the ability to form the charge-transfer species between reduced FNR and NADP+. NADP 112-117 ferredoxin reductase Homo sapiens 104-107 1320378-11 1992 Amino acid sequence homology was detected between the beta-subunit of this cytochrome b and the ferredoxin-NADP+ reductase (FNR) family of reductases in the putative NADPH- and FAD-binding sites. NADP 166-171 ferredoxin reductase Homo sapiens 96-122 1320378-11 1992 Amino acid sequence homology was detected between the beta-subunit of this cytochrome b and the ferredoxin-NADP+ reductase (FNR) family of reductases in the putative NADPH- and FAD-binding sites. NADP 166-171 ferredoxin reductase Homo sapiens 124-127 8251942-4 1993 The FAD and NADPH binding sites have been located on the beta subunit of this molecule, the C-terminal half of which showed weak sequence similarity to other reductases, including the ferredoxin-NADP reductase (FNR) of known structure. NADP 12-17 ferredoxin reductase Homo sapiens 184-209 8251942-4 1993 The FAD and NADPH binding sites have been located on the beta subunit of this molecule, the C-terminal half of which showed weak sequence similarity to other reductases, including the ferredoxin-NADP reductase (FNR) of known structure. NADP 12-17 ferredoxin reductase Homo sapiens 211-214 8396893-3 1993 Adrenodoxin reductase alone oxidized NADPH, reducing O2 to a superoxide radical at a very low rate. NADP 37-42 ferredoxin reductase Homo sapiens 0-21 1567230-1 1992 Ferredoxin reductase (Fd-reductase) supplies reducing equivalents obtained from NADPH to mitochondrial cytochrome P450 enzymes via the small iron-sulfur protein ferredoxin. NADP 80-85 ferredoxin reductase Homo sapiens 0-20 1315050-1 1992 Adrenodoxin reductase (AR; ferridoxin: NADP+ oxidoreductase, EC 1.18.1.2) is a flavoprotein that mediates electron transport from NADPH to all known mitochondrial forms of cytochrome P450. NADP 130-135 ferredoxin reductase Homo sapiens 0-21 1315050-1 1992 Adrenodoxin reductase (AR; ferridoxin: NADP+ oxidoreductase, EC 1.18.1.2) is a flavoprotein that mediates electron transport from NADPH to all known mitochondrial forms of cytochrome P450. NADP 130-135 ferredoxin reductase Homo sapiens 23-25 2403337-0 1990 Nitroreductase reactions of the NADPH: adrenodoxin reductase and the adrenodoxin complex. NADP 32-37 ferredoxin reductase Homo sapiens 39-60 2078639-0 1990 [Stimulation of the NADPH:adrenodoxin reductase diaphorase reaction by adrenodoxin]. NADP 20-25 ferredoxin reductase Homo sapiens 26-47 2078639-1 1990 The diaphorase activity of NADPH: adrenodoxin reductase (EC 1.18.1.2) is stimulated by adrenodoxin. NADP 27-32 ferredoxin reductase Homo sapiens 34-55 2403337-1 1990 NADPH: adrenodoxin reductase (E.C. NADP 0-5 ferredoxin reductase Homo sapiens 7-28 2294024-0 1990 A negative cooperativity between NADPH and adrenodoxin on binding to NADPH:adrenodoxin reductase. NADP 33-38 ferredoxin reductase Homo sapiens 75-96 2294024-0 1990 A negative cooperativity between NADPH and adrenodoxin on binding to NADPH:adrenodoxin reductase. NADP 69-74 ferredoxin reductase Homo sapiens 75-96 2294024-1 1990 Adrenodoxin stimulated the oxidation of NADPH by 1,4-benzoquinone, catalyzed by NADPH:adrenodoxin reductase. NADP 40-45 ferredoxin reductase Homo sapiens 86-107 2993264-0 1985 Phosphorus-31 nuclear magnetic resonance and electronic spectroscopic studies of adrenodoxin reductase and its binary complex with NADP+. NADP 131-136 ferredoxin reductase Homo sapiens 81-102 34081832-5 2021 Co-Immobilization of a ferredoxin NADP + reductase and crotonyl-CoA carboxylase/reductase within a 2,2 -viologen modified hydrogel enabled iterative NADPH recycling and stereoselective formation of (2 S )-ethylmalonyl-CoA, a prospective intermediate towards multi-carbon products from CO 2 , with 92 +- 6 % faradaic efficiency and at a rate of 1.6 +- 0.4 micromol cm -2 h -1 . NADP 149-154 ferredoxin reductase Homo sapiens 23-50 34170697-1 2021 Human isocitrate dehydrogenase (IDH1) and its cancer-associated variant (IDH1 R132H) are rendered electroactive through coconfinement with a rapid NADP(H) recycling enzyme (ferredoxin-NADP+ reductase) in nanopores formed within an indium tin oxide electrode. NADP 147-154 ferredoxin reductase Homo sapiens 173-199 2845396-1 1988 Adrenodoxin reductase is a mitochondrial flavoprotein that receives electrons from NADPH, thus initiating the electron-transport chain serving mitochondrial cytochromes P450. NADP 83-88 ferredoxin reductase Homo sapiens 0-21 3394171-0 1988 [Inhibition of adrenodoxin reductase by NADP+ and NADPH]. NADP 40-45 ferredoxin reductase Homo sapiens 15-36 3394171-0 1988 [Inhibition of adrenodoxin reductase by NADP+ and NADPH]. NADP 50-55 ferredoxin reductase Homo sapiens 15-36 3394171-1 1988 Adrenodoxin reductase (EC 1.18.1.2) catalyzes the oxidation of NADPH by 1.4-benzoquinone. NADP 63-68 ferredoxin reductase Homo sapiens 0-21 3394171-4 1988 NADP+ and NADPH act as mutually exclusive inhibitors relative to reduced adrenodoxin reductase. NADP 0-5 ferredoxin reductase Homo sapiens 73-94 3394171-4 1988 NADP+ and NADPH act as mutually exclusive inhibitors relative to reduced adrenodoxin reductase. NADP 10-15 ferredoxin reductase Homo sapiens 73-94 3593793-1 1987 The reactions of NADPH oxidation by quinones and inorganic complexes catalyzed by NADPH: adrenodoxin reductase were studied. NADP 17-22 ferredoxin reductase Homo sapiens 89-110 3593793-1 1987 The reactions of NADPH oxidation by quinones and inorganic complexes catalyzed by NADPH: adrenodoxin reductase were studied. NADP 82-87 ferredoxin reductase Homo sapiens 89-110 3027455-5 1986 Available evidence indicates that the electron on transfer reaction from NADPH to P-450scc is mediated rapidly by adrenodoxin reductase and p-450 scc. NADP 73-78 ferredoxin reductase Homo sapiens 114-135 3755438-0 1986 Association of ferredoxin-NADP+ reductase with NADP(H) specificity and oxidation-reduction properties. NADP 47-54 ferredoxin reductase Homo sapiens 15-41 3755438-1 1986 The equilibrium properties of the NADP+ binding site of ferredoxin-NADP+ reductase (FNR, or Fd-NADP+ reductase) were examined with regard to specificity in binding, and with regard to the oxidation-reduction properties of the FNR.NADP+ complex. NADP 34-39 ferredoxin reductase Homo sapiens 56-82 3755438-1 1986 The equilibrium properties of the NADP+ binding site of ferredoxin-NADP+ reductase (FNR, or Fd-NADP+ reductase) were examined with regard to specificity in binding, and with regard to the oxidation-reduction properties of the FNR.NADP+ complex. NADP 34-39 ferredoxin reductase Homo sapiens 84-87 3755438-1 1986 The equilibrium properties of the NADP+ binding site of ferredoxin-NADP+ reductase (FNR, or Fd-NADP+ reductase) were examined with regard to specificity in binding, and with regard to the oxidation-reduction properties of the FNR.NADP+ complex. NADP 34-39 ferredoxin reductase Homo sapiens 226-229 3755438-1 1986 The equilibrium properties of the NADP+ binding site of ferredoxin-NADP+ reductase (FNR, or Fd-NADP+ reductase) were examined with regard to specificity in binding, and with regard to the oxidation-reduction properties of the FNR.NADP+ complex. NADP 67-72 ferredoxin reductase Homo sapiens 84-87 3755438-7 1986 Fd-NADP+ reductase was found to form a high-affinity two-electron reduced complex (FNR.NADPH) with a NADPH; complex formation was associated with appearance of long-wavelength charge-transfer bands. NADP 87-92 ferredoxin reductase Homo sapiens 83-86 3755438-7 1986 Fd-NADP+ reductase was found to form a high-affinity two-electron reduced complex (FNR.NADPH) with a NADPH; complex formation was associated with appearance of long-wavelength charge-transfer bands. NADP 101-106 ferredoxin reductase Homo sapiens 83-86 3755438-8 1986 Kd of FNR.NADPH complex was about 6% the Kd of oxidized FNR.NADP+ complex. NADP 10-15 ferredoxin reductase Homo sapiens 6-9 3755438-8 1986 Kd of FNR.NADPH complex was about 6% the Kd of oxidized FNR.NADP+ complex. NADP 10-15 ferredoxin reductase Homo sapiens 56-59 3755438-8 1986 Kd of FNR.NADPH complex was about 6% the Kd of oxidized FNR.NADP+ complex. NADP 60-65 ferredoxin reductase Homo sapiens 6-9 3755438-8 1986 Kd of FNR.NADPH complex was about 6% the Kd of oxidized FNR.NADP+ complex. NADP 60-65 ferredoxin reductase Homo sapiens 56-59 3755438-9 1986 As predicted by the lower Kd, the Em for reduction of FNR.NADP+ complex to the charge-transfer complex was about 40 mV more positive than the potential of the NADP+/NADPH couple. NADP 58-63 ferredoxin reductase Homo sapiens 54-57 3755438-9 1986 As predicted by the lower Kd, the Em for reduction of FNR.NADP+ complex to the charge-transfer complex was about 40 mV more positive than the potential of the NADP+/NADPH couple. NADP 159-164 ferredoxin reductase Homo sapiens 54-57 3755438-9 1986 As predicted by the lower Kd, the Em for reduction of FNR.NADP+ complex to the charge-transfer complex was about 40 mV more positive than the potential of the NADP+/NADPH couple. NADP 165-170 ferredoxin reductase Homo sapiens 54-57 3755438-10 1986 Rapid kinetic studies supported description of the charge-transfer complex as primarily oxidized FNR.NADPH. NADP 101-106 ferredoxin reductase Homo sapiens 97-100 3004338-2 1986 O2- was produced by gamma irradiation of formate solutions, by the action of xanthine oxidase on hypoxanthine and O2, and by the action of ferredoxin reductase on NADPH and paraquat in the presence of O2. NADP 163-168 ferredoxin reductase Homo sapiens 139-159 2993264-1 1985 The 31P NMR spectra of NADPH-adrenodoxin reductase and its complex with NADP+ are reported. NADP 72-77 ferredoxin reductase Homo sapiens 29-50 2993264-4 1985 Further, one of the doublets of phosphorus nuclei of the pyrophosphate group of bound NADP+ in the complex of adrenodoxin reductase and NADP+ was considerably shifted upfield in comparison with that of free NADP+. NADP 86-91 ferredoxin reductase Homo sapiens 110-131 2993264-4 1985 Further, one of the doublets of phosphorus nuclei of the pyrophosphate group of bound NADP+ in the complex of adrenodoxin reductase and NADP+ was considerably shifted upfield in comparison with that of free NADP+. NADP 136-141 ferredoxin reductase Homo sapiens 110-131 2993264-4 1985 Further, one of the doublets of phosphorus nuclei of the pyrophosphate group of bound NADP+ in the complex of adrenodoxin reductase and NADP+ was considerably shifted upfield in comparison with that of free NADP+. NADP 136-141 ferredoxin reductase Homo sapiens 110-131 7150671-2 1982 Upon reconstitution of the enzymatically complete system in the presence of NADPH the formation of a ternary protein complex was accompanied by a 2-10-fold increase of the Kd values as compared to the formation of binary adrenodoxin reductase . NADP 76-81 ferredoxin reductase Homo sapiens 221-242 6746626-2 1984 Ferredoxin:NADP+ oxidoreductase (ferredoxin: NADP+ reductase, EC 1.18.1.2) was shown to form a ternary complex with its substrates ferredoxin (Fd) and NADP(H), but the ternary complex was less stable than the separate binary complexes. NADP 11-15 ferredoxin reductase Homo sapiens 33-60 3917922-0 1985 The NADP+-binding site of ferredoxin-NADP+ reductase. NADP 4-9 ferredoxin reductase Homo sapiens 26-52 6625616-1 1983 To determine if the interaction between ferredoxin and ferredoxin:NADP reductase is similar to the interaction between the purified proteins when the ferrodoxin:NADP reductase is membrane bound, the effect of pH, salt, and coupling state on the Km for ferredoxin in NADP reduction by chloroplast membranes has been examined. NADP 66-70 ferredoxin reductase Homo sapiens 40-50 6625616-1 1983 To determine if the interaction between ferredoxin and ferredoxin:NADP reductase is similar to the interaction between the purified proteins when the ferrodoxin:NADP reductase is membrane bound, the effect of pH, salt, and coupling state on the Km for ferredoxin in NADP reduction by chloroplast membranes has been examined. NADP 66-70 ferredoxin reductase Homo sapiens 55-65 7171648-3 1982 At ferredoxin concentrations studied an addition of NADP+ to the system which makes possible electron transfer from ferredoxin to ferredoxin-NADP+-reductase increases the rate of overall electron transport across the chain. NADP 52-57 ferredoxin reductase Homo sapiens 130-156 8135-0 1976 A lysyl residue at the NADP binding site of ferredoxin-NADP reductase. NADP 23-27 ferredoxin reductase Homo sapiens 44-69 16008-2 1977 Adrenodoxin reductase, the flavoprotein moiety of the adrenal cortex mitochondrial steroid hydroxylating system, participates in adrenodoxin-dependent cytochrome c and adrenodoxin-independent ferricyanide reduction, with NADPH as electron donor for both of these 1-electron reductions. NADP 221-226 ferredoxin reductase Homo sapiens 0-21 12171-4 1976 We have found that when adrenodoxin: adrenodoxin reductase ratios are varied by increasing the adrenodoxin concentration, with adrenodoxin reductase held constant, an increasing rate of cytochrome c reduction, with NADPH as reductant, is seen up to a ratio of 1:1, indicating that cytochrome c reduction occurs via the protein-protein complex. NADP 215-220 ferredoxin reductase Homo sapiens 37-58 12171-4 1976 We have found that when adrenodoxin: adrenodoxin reductase ratios are varied by increasing the adrenodoxin concentration, with adrenodoxin reductase held constant, an increasing rate of cytochrome c reduction, with NADPH as reductant, is seen up to a ratio of 1:1, indicating that cytochrome c reduction occurs via the protein-protein complex. NADP 215-220 ferredoxin reductase Homo sapiens 127-148 12171-10 1976 Titration of the adrenodoxin reductase-adrenodoxin complex with the physiologic reductant, NADPH, was followed by EPR and visible spectra, and yielded an order of reduction of the components identical with that seen when NADH was used as reductant. NADP 91-96 ferredoxin reductase Homo sapiens 17-38 6475-10 1976 Oxidized adrenodoxin reductase binds NADP+ much more weakly (Kdiss=1.4 X 10(-5) M) than does reduced adrenodoxin reductase, with a single binding site. NADP 37-42 ferredoxin reductase Homo sapiens 9-30 6475-2 1976 Anaerobic reduction of the flavoprotein adrenodoxin reductase with NADPH yields a spectrum with long wavelength absorbance, 750 nm and higher. NADP 67-72 ferredoxin reductase Homo sapiens 40-61 6475-4 1976 This spectrum is produced by titration of oxidized adrenodoxin reductase with NADPH, or of dithionite-reduced adrenodoxin reductase with NADP+. NADP 78-83 ferredoxin reductase Homo sapiens 51-72 6475-4 1976 This spectrum is produced by titration of oxidized adrenodoxin reductase with NADPH, or of dithionite-reduced adrenodoxin reductase with NADP+. NADP 137-142 ferredoxin reductase Homo sapiens 110-131 6475-7 1976 The species formed on NADPH reduction appears to be a two-electron-containing complex, with a low dissociation constant, between reduced adrenodoxin reductase and NADP+, designated ARH2-NADP+. NADP 22-27 ferredoxin reductase Homo sapiens 137-158 6475-7 1976 The species formed on NADPH reduction appears to be a two-electron-containing complex, with a low dissociation constant, between reduced adrenodoxin reductase and NADP+, designated ARH2-NADP+. NADP 163-168 ferredoxin reductase Homo sapiens 137-158 6475-7 1976 The species formed on NADPH reduction appears to be a two-electron-containing complex, with a low dissociation constant, between reduced adrenodoxin reductase and NADP+, designated ARH2-NADP+. NADP 22-26 ferredoxin reductase Homo sapiens 137-158 6475-8 1976 Titration of dithionite-reduced adrenodoxin reductase with NADPH also produces a distinctive spectrum, with a sharp endpoint at 1 NADPH added per reduced flavin, indicating formation of a four-electron-containing complex between reduced adrenodoxin reductase and NADPH. NADP 59-64 ferredoxin reductase Homo sapiens 32-53 6475-8 1976 Titration of dithionite-reduced adrenodoxin reductase with NADPH also produces a distinctive spectrum, with a sharp endpoint at 1 NADPH added per reduced flavin, indicating formation of a four-electron-containing complex between reduced adrenodoxin reductase and NADPH. NADP 59-64 ferredoxin reductase Homo sapiens 237-258 6475-8 1976 Titration of dithionite-reduced adrenodoxin reductase with NADPH also produces a distinctive spectrum, with a sharp endpoint at 1 NADPH added per reduced flavin, indicating formation of a four-electron-containing complex between reduced adrenodoxin reductase and NADPH. NADP 130-135 ferredoxin reductase Homo sapiens 32-53 6475-8 1976 Titration of dithionite-reduced adrenodoxin reductase with NADPH also produces a distinctive spectrum, with a sharp endpoint at 1 NADPH added per reduced flavin, indicating formation of a four-electron-containing complex between reduced adrenodoxin reductase and NADPH. NADP 130-135 ferredoxin reductase Homo sapiens 237-258 6475-8 1976 Titration of dithionite-reduced adrenodoxin reductase with NADPH also produces a distinctive spectrum, with a sharp endpoint at 1 NADPH added per reduced flavin, indicating formation of a four-electron-containing complex between reduced adrenodoxin reductase and NADPH. NADP 130-135 ferredoxin reductase Homo sapiens 32-53 6475-8 1976 Titration of dithionite-reduced adrenodoxin reductase with NADPH also produces a distinctive spectrum, with a sharp endpoint at 1 NADPH added per reduced flavin, indicating formation of a four-electron-containing complex between reduced adrenodoxin reductase and NADPH. NADP 130-135 ferredoxin reductase Homo sapiens 237-258 6475-9 1976 Titration of adrenodoxin reductase with NADH, instead of NADPH, provides a curved titration plot rather than the sharp break seen with NADPH, and permits calculation of a potential for the AR/ARH2 couple of -0.291 V, close to that of NAD(P)H (-0.316 V). NADP 135-140 ferredoxin reductase Homo sapiens 13-34 6475-12 1976 From this alteration in potential, a Kdiss of 1.0 X 10(-8) M for binding of NADP+ to reduced adrenodoxin reductase is calculated. NADP 76-81 ferredoxin reductase Homo sapiens 93-114 6475-13 1976 It is concluded that the strong binding of NADP+ to reduced adrenodoxin reductase provides the thermodynamic driving force for formation of a fully reduced flavoprotein form under conditions wherein incomplete reduction would otherwise be expected. NADP 43-48 ferredoxin reductase Homo sapiens 60-81 6475-14 1976 Stopped flow studies demonstrate that reduction of adrenodoxin reductase by equimolar NADPH to form the ARH2-NADP+ complex is first order (k=28 s-1). NADP 86-91 ferredoxin reductase Homo sapiens 51-72 1176457-5 1975 Due to the rapid autooxidizability of reduced adrenodoxin, only a small fraction of electrons conveyed from NADPH to adrenodoxin by way of adrenodoxin reductase was utilized for the deoxycorticosterone 11beta-hydroxylase reaction under the conditions employed. NADP 108-113 ferredoxin reductase Homo sapiens 139-160 33381377-4 2020 One of the enzymes is the photosynthetic flavoenzyme, ferredoxin NADP+ reductase (FNR), which catalyzes the quasi-reversible electrochemical recycling of NADP(H) and serves as the transducer. NADP 65-69 ferredoxin reductase Homo sapiens 82-85 32215444-6 2020 Binding of the FNR:PetF complex to the substrate NADP+ results in bulk-like solvent dynamics of 7 ps, showing that formation of the ternary complex is entropically favored. NADP 49-54 ferredoxin reductase Homo sapiens 15-18 32215444-8 2020 Complex formation between the positively charged FNR:NADP+ pre-complex and the negatively charged PetF is not only entropically favored, but in addition the solvent reorganization into more bulk-like water assists the molecular recognition process. NADP 53-58 ferredoxin reductase Homo sapiens 49-52 31729224-13 2019 The photogenerated MV+ by the two hybrid photosystems is used to catalyze H2-evolution in the presence of Pt nanoparticle catalysts, and to mediate the reduction of NADP+ to NADPH in the presence of ferredoxin-NADP+ reductase, FNR. NADP 166-170 ferredoxin reductase Homo sapiens 200-226 31729224-13 2019 The photogenerated MV+ by the two hybrid photosystems is used to catalyze H2-evolution in the presence of Pt nanoparticle catalysts, and to mediate the reduction of NADP+ to NADPH in the presence of ferredoxin-NADP+ reductase, FNR. NADP 175-180 ferredoxin reductase Homo sapiens 200-226