PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 17892308-2 2007 MSR contains one FAD and one FMN cofactor per polypeptide and functions in the sequential transfer of reducing equivalents from NADPH to MS via its flavin centers. NADP 128-133 formin 1 Homo sapiens 29-32 15180983-7 2004 The combined results from pre-steady-state and EPR experiments revealed that this was associated with a lesser degree of FMN shielding in the NADP(+)-bound state as compared with wild type. NADP 142-149 formin 1 Homo sapiens 121-124 17411075-2 2007 NADPH analogues and fragments have been used to map those regions of this substrate that are important in eliciting a conformational change, observed in both the fluorescence emission of the flavin cofactors of the enzyme and the EPR spectra of the FMN flavosemiquinone state. NADP 0-5 formin 1 Homo sapiens 249-252 15180983-9 2004 It facilitates NADP(+) release to prevent this step from being rate-limiting, and it enables NADP(H) to properly regulate a conformational equilibrium involving the FMN subdomain that controls reactivity of the FMN cofactor in electron transfer. NADP 15-22 formin 1 Homo sapiens 165-168 15180983-9 2004 It facilitates NADP(+) release to prevent this step from being rate-limiting, and it enables NADP(H) to properly regulate a conformational equilibrium involving the FMN subdomain that controls reactivity of the FMN cofactor in electron transfer. NADP 15-22 formin 1 Homo sapiens 211-214 15180983-9 2004 It facilitates NADP(+) release to prevent this step from being rate-limiting, and it enables NADP(H) to properly regulate a conformational equilibrium involving the FMN subdomain that controls reactivity of the FMN cofactor in electron transfer. NADP 93-100 formin 1 Homo sapiens 165-168 15180983-9 2004 It facilitates NADP(+) release to prevent this step from being rate-limiting, and it enables NADP(H) to properly regulate a conformational equilibrium involving the FMN subdomain that controls reactivity of the FMN cofactor in electron transfer. NADP 93-100 formin 1 Homo sapiens 211-214 11022049-1 2000 Transfer of reducing equivalents from NADPH to the cytochromes P450 is mediated by NADPH-cytochrome P450 oxidoreductase, which contains stoichiometric amounts of tightly bound FMN and FAD. NADP 38-43 formin 1 Homo sapiens 176-179 12646269-7 2003 For the FAD/FMN domain, the reduction of the FAD-FMN pair of the oxidized enzyme with NADPH proceeded by both one-electron equivalent and two-electron equivalent mechanisms. NADP 86-91 formin 1 Homo sapiens 12-15 12777376-8 2003 NADPH reduction of the FAD and FMN redox centers by the CaM-bound flavin domains was studied by stopped-flow and rapid scan spectrometry. NADP 0-5 formin 1 Homo sapiens 31-34 11926825-5 2002 The slow phase (1/tau = 55 +/- 2 s(-1)) observed in the absorption transients obtained with CPR reduced at the two-electron level with NADPH reports on internal electron transfer: FAD(sq)-FMN(sq) --> FAD(ox)-FMN(hq). NADP 135-140 formin 1 Homo sapiens 188-191 11926825-5 2002 The slow phase (1/tau = 55 +/- 2 s(-1)) observed in the absorption transients obtained with CPR reduced at the two-electron level with NADPH reports on internal electron transfer: FAD(sq)-FMN(sq) --> FAD(ox)-FMN(hq). NADP 135-140 formin 1 Homo sapiens 211-214 11926825-7 2002 Temperature perturbation experiments with CPR reduced with 10-fold molar excess of NADPH produce monophasic absorption transients (1/tau = 20 +/- 0.2 s(-1)) reporting on internal electron transfer: FAD(sq)-FMN(hq) --> FAD(hq)-FMN(sq). NADP 83-88 formin 1 Homo sapiens 206-209 11926825-7 2002 Temperature perturbation experiments with CPR reduced with 10-fold molar excess of NADPH produce monophasic absorption transients (1/tau = 20 +/- 0.2 s(-1)) reporting on internal electron transfer: FAD(sq)-FMN(hq) --> FAD(hq)-FMN(sq). NADP 83-88 formin 1 Homo sapiens 229-232 11926825-12 2002 Replacement of Trp-676 with His-676 reduces approximately 2-fold the observed rate of internal electron transfer in two-electron-reduced enzyme, whereas the observed rate for FAD(sq)-FMN(hq) --> FAD(hq)-FMN(sq) transfer is increased approximately 13-fold in the W676H mutant reduced with a 10-fold molar excess of NADPH. NADP 317-322 formin 1 Homo sapiens 183-186 11329263-1 2001 The reduction by NADPH of the FAD and FMN redox centers in human cytochrome P450 reductase and its component domains has been studied by rapid-mixing, stopped-flow spectroscopy. NADP 17-22 formin 1 Homo sapiens 38-41 9535883-10 1998 In the case of 8-CN-OYE I, it was shown that the rate of reduction of the enzyme bound flavin by NADPH is approximately 40 times faster, and the rate of reoxidation of reduced enzyme bound flavin by oxygen is an order of magnitude slower than with the normal FMN enzyme. NADP 97-102 formin 1 Homo sapiens 259-262 10924903-2 2000 The recombinant neuronal nitric oxide synthase (nNOS) reductase domain, which contains the FAD-FMN prosthetic group pair and calmodulin-binding site, catalyzed aerobic NADPH-oxidation in the presence of the model quinone compound menadione (MD), including antitumor mitomycin C (Mit C) and adriamycin (Adr). NADP 168-173 formin 1 Homo sapiens 95-98 10428800-5 1999 Characterization of the FMN-depleted mutants showed that bound FMN was essential for reduction of the nNOS heme or cytochrome c, but not for ferricyanide or dichlorophenolindolphenol, and established that the electron transfer path in nNOS is NADPH to FAD to FMN to heme. NADP 243-248 formin 1 Homo sapiens 24-27 10428800-6 1999 Steady-state and stopped-flow kinetic analysis revealed a novel role for bound FMN in suppressing FAD reduction by NADPH. NADP 115-120 formin 1 Homo sapiens 79-82 9485308-4 1998 This subunit contains FMN as the flavin cofactor which exhibits the properties of Flavin 2 of glutamate synthase: reactivity with sulfite to yield a flavin-N(5)-sulfite addition product (Kd = 2.6 +/- 0.22 mM), lack of reactivity with NADPH, reduction by L-glutamate, and reoxidation by 2-oxoglutarate and glutamine. NADP 234-239 formin 1 Homo sapiens 22-25 9010603-2 1996 High ionic strength facilitated electron transfer from NADPH to the FMN moiety of the reductase domain (BMR) of P450BM-3 and did not affect the first electron transfer from FMN to the heme in the holoenzyme. NADP 55-60 formin 1 Homo sapiens 68-71 9374858-3 1997 Results indicate that electron flow occurs from the NADPH donor through FAD, then FMN and on to the heme center where fatty acid substrate is bound and monooxygenation occurs. NADP 52-57 formin 1 Homo sapiens 82-85 3015206-10 1986 The other protomer, containing only FMN and the clusters 2, 3 and 4, is supposed to catalyse the oxidation of NADPH. NADP 110-115 formin 1 Homo sapiens 36-39 2879563-3 1986 6-Azido-FMN Old Yellow Enzyme is converted to the 6-amino-FMN enzyme by aerobic turnover with NADPH, and 6-azido-FAD D-amino acid oxidase is converted to the 6-amino-FAD enzyme by treatment with D-alanine. NADP 94-99 formin 1 Homo sapiens 8-11 2879563-3 1986 6-Azido-FMN Old Yellow Enzyme is converted to the 6-amino-FMN enzyme by aerobic turnover with NADPH, and 6-azido-FAD D-amino acid oxidase is converted to the 6-amino-FAD enzyme by treatment with D-alanine. NADP 94-99 formin 1 Homo sapiens 58-61 2064373-7 1991 The P450cam putidaredoxin reductase contains only FAD and is quite specific for NADH (35, 39); the P450meg megaredoxin reductase contains only FMN and is specific for NADPH (59, 60). NADP 167-172 formin 1 Homo sapiens 143-146 32812692-4 2021 Here, extensive molecular dynamics simulations and interaction network analysis reveal that the 49th isoleucine is a crucial residue that allosterically regulates the dynamics between the FMN and NADP(H) binding domains. NADP 196-203 formin 1 Homo sapiens 188-191 3925989-1 1985 The mechanism of electron transfer from NADPH to cytochrome P-450 through FAD and FMN of the reductase is largely unknown. NADP 40-45 formin 1 Homo sapiens 82-85 27806563-6 2016 The Y118A SsuE FMN cofactor was reduced with approximately 1 equiv of NADPH in anaerobic titration experiments, and the flavin remained bound following reduction. NADP 70-75 formin 1 Homo sapiens 15-18 29308883-1 2018 Conformational changes in NADPH-cytochrome P450 oxidoreductase (CYPOR) associated with electron transfer from NADPH to electron acceptors via FAD and FMN have been investigated via structural studies of the four-electron-reduced NADP+-bound enzyme and kinetic and structural studies of mutants that affect the conformation of the mobile Gly631-Asn635 loop (Asp632 loop). NADP 26-31 formin 1 Homo sapiens 150-153 29308883-1 2018 Conformational changes in NADPH-cytochrome P450 oxidoreductase (CYPOR) associated with electron transfer from NADPH to electron acceptors via FAD and FMN have been investigated via structural studies of the four-electron-reduced NADP+-bound enzyme and kinetic and structural studies of mutants that affect the conformation of the mobile Gly631-Asn635 loop (Asp632 loop). NADP 229-234 formin 1 Homo sapiens 150-153 26634408-2 2015 The SsuE enzyme is an NADPH-dependent FMN reductase that provides reduced flavin to the SsuD monooxygenase enzyme. NADP 22-27 formin 1 Homo sapiens 38-41 23332101-1 2013 Methionine synthase reductase (MSR) and cytochrome P450 reductase (CPR) transfer reducing equivalents from NADPH via an FAD and FMN cofactor to a redox partner protein. NADP 107-112 formin 1 Homo sapiens 128-131 25194416-2 2014 Both FAD and FMN flavin groups mediate the transfer of NADPH derived electrons to NOS. NADP 55-60 formin 1 Homo sapiens 13-16 24737326-7 2014 Our three-dimensional reconstruction of the intact nNOS-CaM complex reveals a closed conformation and a cross-monomer arrangement with the FMN domain rotated away from the NADPH-FAD center, toward the oxygenase dimer. NADP 172-177 formin 1 Homo sapiens 139-142 20529840-5 2010 The bridging interaction appeared to control FMN subdomain interactions with both its electron donor (NADPH-FAD subdomain) and electron acceptor (heme domain) partner subdomains in nNOS. NADP 102-107 formin 1 Homo sapiens 45-48 22891242-7 2012 Upon complete reduction by NADPH, the conformational equilibrium shifts toward the compact form protecting the reduced FMN cofactor from engaging in unspecific electron transfer reaction. NADP 27-32 formin 1 Homo sapiens 119-122 20188793-5 2010 Computational molecular docking experiments with a FMN free structural model of POR revealed that an external FMN could be docked in close proximity to the FAD moiety and receive electrons donated by NADPH. NADP 200-205 formin 1 Homo sapiens 51-54 20188793-5 2010 Computational molecular docking experiments with a FMN free structural model of POR revealed that an external FMN could be docked in close proximity to the FAD moiety and receive electrons donated by NADPH. NADP 200-205 formin 1 Homo sapiens 110-113