PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 1287650-5 1992 RSMG enzyme is more reactive towards Bz-val-gly-arg-pNA and tosyl-gly-pro-arg-pNA, preferential chromogenic substrates for trypsin-like proteases and thrombin, respectively. BZ-VAL-GLY-ARG-PNA 37-55 coagulation factor II Rattus norvegicus 150-158 1287650-5 1992 RSMG enzyme is more reactive towards Bz-val-gly-arg-pNA and tosyl-gly-pro-arg-pNA, preferential chromogenic substrates for trypsin-like proteases and thrombin, respectively. tosyl-gly-pro-arg-pna 60-81 coagulation factor II Rattus norvegicus 150-158 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 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 23-25 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