Aromatic substitution of the FAD-shielding tryptophan reveals its differential role in regulating electron flux in methionine synthase reductase and cytochrome P450 reductase

FEBS Journal

Volumn 280, Issue 6, 2013, Pages 1460-1474

  Meints, Carla E ^a   Simtchouk, Svetlana ^a   Wolthers, Kirsten R ^a  

^a UNIVERSITY OF BRITISH COLUMBIA   (Canada)

Author keywords

cytochrome P450 reductase; electron transfer; flavin; methionine synthase reductase; stopped flow spectroscopy

Indexed keywords

CYTOCHROME C; CYTOCHROME P450 REDUCTASE; DISEMIQUINONE; FLAVINE ADENINE NUCLEOTIDE; METHIONINE SYNTHASE REDUCTASE; QUINONE DERIVATIVE; TRYPTOPHAN; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; CONTROLLED STUDY; ELECTRON TRANSPORT; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME REGULATION; PRIORITY JOURNAL; PROTEIN STRUCTURE; STEADY STATE; STRUCTURE ACTIVITY RELATION; SURFACE CHARGE;

AMINO ACID SUBSTITUTION; AMINO ACIDS, AROMATIC; CATALYSIS; CYTOCHROME C GROUP; DINITROCRESOLS; ELECTRON TRANSPORT; ESCHERICHIA COLI; FERREDOXIN-NADP REDUCTASE; FLAVIN-ADENINE DINUCLEOTIDE; KINETICS; MUTAGENESIS, SITE-DIRECTED; NADP; NADPH-FERRIHEMOPROTEIN REDUCTASE; OXIDATION-REDUCTION; PLASMIDS; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; THERMODYNAMICS; TITRIMETRY; TRYPTOPHAN;

EID: 84875363969     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.12141     Document Type: Article

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