Proximal FAD histidine residue influences interflavin electron transfer in cytochrome P450 reductase and methionine synthase reductase

Archives of Biochemistry and Biophysics

Volumn 547, Issue , 2014, Pages 18-26

  Meints, Carla E ^a   Parke, Sarah M ^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 C3; CYTOCHROME P450 REDUCTASE; FLAVINE ADENINE NUCLEOTIDE; HISTIDINE; HYDROQUINONE; METHIONINE SYNTHASE REDUCTASE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

ARTICLE; BINDING AFFINITY; COENZYME; DNA SEQUENCE; ELECTRON TRANSPORT; ENZYME METABOLISM; ENZYME PURIFICATION; FLOW MEASUREMENT; HUMAN; HYDROGEN BOND; MUTAGENESIS; OXIDATION REDUCTION POTENTIAL; OXIDATION REDUCTION STATE; POTENTIOMETRY; PRIORITY JOURNAL; PROTEIN EXPRESSION; SITE DIRECTED MUTAGENESIS; STEADY STATE;

CYTOCHROME P450 REDUCTASE; ELECTRON TRANSFER; FLAVIN; METHIONINE SYNTHASE REDUCTASE; STOPPED-FLOW SPECTROSCOPY;

AMINO ACID SUBSTITUTION; CATALYTIC DOMAIN; ELECTRON TRANSPORT; FERREDOXIN-NADP REDUCTASE; FLAVIN MONONUCLEOTIDE; FLAVIN-ADENINE DINUCLEOTIDE; HISTIDINE; HUMANS; MODELS, MOLECULAR; NADPH-FERRIHEMOPROTEIN REDUCTASE; OXIDATION-REDUCTION; PROTEIN STRUCTURE, TERTIARY;

EID: 84896538414     PISSN: 00039861     EISSN: 10960384     Source Type: Journal    
DOI: 10.1016/j.abb.2014.02.009     Document Type: Article

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