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Volumn 409, Issue 1, 2003, Pages 102-112

Structural alterations of the heme environment of cytochrome P450cam and the Y96F mutant as deduced by resonance Raman spectroscopy

(5) Niaura, Gediminas a Reipa, Vytas a Mayhew, Martin P a Holden, Marcia a Vilker, Vincent L a

a NATIONAL INSTITUTE OF STANDARDS AND TECHNOLOGY (United States)

Author keywords

Camphor; Cytochrome P450; Raman spectroscopy; Spin equilibrium; Styrene

Indexed keywords

CAMPHOR; CAMPHOR 5 MONOOXYGENASE; CYTOCHROME P450; HEME; MUTANT PROTEIN; PHENYLALANINE; PUTIDAREDOXIN; PYRROLE DERIVATIVE; STYRENE;

ARTICLE; BINDING AFFINITY; CALCULATION; ELECTRON TRANSPORT; ENANTIOMER; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME SUBSTRATE; EQUILIBRIUM CONSTANT; HYDROXYLATION; MUTATION; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; RAMAN SPECTROMETRY; STEREOCHEMISTRY; WILD TYPE;

BIOCHEMISTRY; CAMPHOR; CAMPHOR 5-MONOOXYGENASE; ESCHERICHIA COLI; HEME; HYDROXYLATION; IRON; KINETICS; MODELS, CHEMICAL; MODELS, MOLECULAR; MUTATION; PLASMIDS; PORPHYRINS; PROTEIN BINDING; PROTEIN CONFORMATION; SPECTRUM ANALYSIS, RAMAN; STYRENE; SUBSTRATE SPECIFICITY;

DRYOBALANOPS;

EID: 0037227645 PISSN: 00039861 EISSN: None Source Type: Journal
DOI: 10.1016/S0003-9861(02)00581-7 Document Type: Article

Times cited : (11)

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