Distinct conformational behaviors of four mammalian dual-flavin reductases (cytochrome P450 reductase, methionine synthase reductase, neuronal nitric oxide synthase, endothelial nitric oxide synthase) determine their unique catalytic profiles

FEBS Journal

Volumn 281, Issue 23, 2014, Pages 5325-5340

  Haque, Mohammad M ^a   Bayachou, Mekki ^b   Tejero, Jesus ^c   Kenney, Claire T ^a   Pearl, Naw M ^d   Im, Sang Choul ^d   Waskell, Lucy ^d   Stuehr, Dennis J ^a  

^a LERNER RESEARCH INSTITUTE   (United States)

^b CLEVELAND STATE UNIVERSITY   (United States)

^c UNIVERSITY OF PITTSBURGH   (United States)

^d UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

Author keywords

Conformational equilibrium; Electron transfer; Flavoprotein; Kinetic model; Nitric oxide

Indexed keywords

CYTOCHROME C; CYTOCHROME P450 REDUCTASE; ENDOTHELIAL NITRIC OXIDE SYNTHASE; FLAVOPROTEIN; METHIONINE SYNTHASE REDUCTASE; NEURONAL NITRIC OXIDE SYNTHASE; NITRIC OXIDE SYNTHASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE DEHYDROGENASE; FERREDOXIN NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE REDUCTASE; NOS1 PROTEIN, HUMAN; NOS3 PROTEIN, HUMAN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE FERRIHEMOPROTEIN REDUCTASE;

ARTICLE; CATALYSIS; CONFORMATIONAL TRANSITION; ELECTRON TRANSPORT; ENZYME ACTIVITY; KINETICS; PROTEIN DOMAIN; SPECTROSCOPY; STEADY STATE; BIOCATALYSIS; CHEMISTRY; HUMAN; OXIDATION REDUCTION REACTION; PROTEIN CONFORMATION;

MAMMALIA;

BIOCATALYSIS; CYTOCHROMES C; FERREDOXIN-NADP REDUCTASE; HUMANS; NADPH-FERRIHEMOPROTEIN REDUCTASE; NITRIC OXIDE SYNTHASE TYPE I; NITRIC OXIDE SYNTHASE TYPE III; OXIDATION-REDUCTION; PROTEIN CONFORMATION;

EID: 84918841685     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.13073     Document Type: Article

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