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Biochemistry

Volumn 40, Issue 45, 2001, Pages 13574-13582

The structure and biochemistry of NADH-dependent cytochrome b5 reductase are now consistent

(3) Bewley, M C a Marohnic, C C b Barber, M J b,c

a BROOKHAVEN NATIONAL LABORATORY (United States)

b UNIVERSITY OF SOUTH FLORIDA (United States)

c H LEE MOFFITT CANCER CENTER AND RESEARCH INSTITUTE (United States)

Author keywords

[No Author keywords available]

Indexed keywords

NORMAL FLAVIN BEHAVIOR;

AMINO ACIDS; BIOASSAY; BIOCHEMISTRY; CRYSTAL STRUCTURE; DISEASES; ELECTRONS; HEMOGLOBIN; MUTAGENESIS;

ENZYMES;

AMINO ACID; CYSTEINE; CYTOCHROME B5 REDUCTASE; GLUTAMIC ACID; LYSINE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; BIOCHEMISTRY; CATALYSIS; CATALYST; ENZYME STRUCTURE; METHEMOGLOBINEMIA; NONHUMAN; OPTICAL RESOLUTION; PRIORITY JOURNAL; PROTEIN FOLDING; RAT; REACTION ANALYSIS; REDUCTION; STRUCTURE ANALYSIS; SWINE;

AMINO ACID SEQUENCE; ANIMALS; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; CYTOCHROME REDUCTASES; CYTOCHROME-B(5) REDUCTASE; HUMANS; LYSINE; METHEMOGLOBINEMIA; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; NAD; PROTEIN CONFORMATION; RATS; SEQUENCE HOMOLOGY, AMINO ACID; SWINE;

SUS SCROFA;

EID: 0035856561 PISSN: 00062960 EISSN: None Source Type: Journal
DOI: 10.1021/bi0106336 Document Type: Article

Times cited : (72)

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