The catalytic mechanism of cytochrome P450 BM3 involves a 6 Å movement of the bound substrate on reduction

Nature Structural Biology

Volumn 3, Issue 5, 1996, Pages 414-417

  Modi, S ^a   Sutcliffe, M J ^a   Primrose, W U ^a   Lian, L Y ^a   Roberts, G C K ^a  

^a UNIVERSITY OF LEICESTER   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME P450;

ARTICLE; CONFORMATIONAL TRANSITION; ELECTRON SPIN RESONANCE; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME MECHANISM; ENZYME SUBSTRATE COMPLEX; HYDROXYLATION; PRIORITY JOURNAL; PROTEIN DOMAIN;

BACILLUS MEGATERIUM; BACTERIAL PROTEINS; CAMPHOR 5-MONOOXYGENASE; COMPUTER SIMULATION; CYTOCHROME P-450 ENZYME SYSTEM; HYDROXYLATION; LAURATES; MAGNETIC RESONANCE SPECTROSCOPY; MIXED FUNCTION OXYGENASES; MODELS, MOLECULAR; MOVEMENT; OXIDATION-REDUCTION;

EID: 0029876059     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb0596-414     Document Type: Article

References (0)