Enzyme-catalyzed dehalogenation of pentachloroethane: Why f87w-cytochrome p450cam is faster than wild type

Protein Engineering, Design and Selection

Volumn 8, Issue 8, 1995, Pages 801-807

  Manchester, John I ^a   Ornstein, Rick L ^a  

^a PACIFIC NORTHWEST NATIONAL LABORATORY   (United States)

Author keywords

Cytochrome P450cam; Molecular dynamics; Pentachloroethane; Protein; Reductive dehalogenation; Simulation

Indexed keywords

CYTOCHROME P450; HALOGENATED HYDROCARBON; MICROBIAL ENZYME; MUTANT PROTEIN; PENTACHLOROETHANE;

ARTICLE; BINDING SITE; CHEMICAL BOND; CONTROLLED STUDY; DECHLORINATION; DEHALOGENATION; ECOSYSTEM; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME CONFORMATION; MOLECULAR DYNAMICS; PRIORITY JOURNAL; STEREOSPECIFICITY; WASTE MANAGEMENT;

BINDING SITES; CAMPHOR 5-MONOOXYGENASE; COMPARATIVE STUDY; COMPUTER SIMULATION; CRYSTALLOGRAPHY, X-RAY; CYTOCHROME P-450 ENZYME SYSTEM; ETHANE; HEME; HYDROCARBONS, CHLORINATED; KINETICS; MIXED FUNCTION OXYGENASES; MODELS, MOLECULAR; PHENYLALANINE; POINT MUTATION; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SUPPORT, NON-U.S. GOV'T; SUPPORT, U.S. GOV'T, NON-P.H.S.;

EID: 0028845403     PISSN: 17410126     EISSN: None     Source Type: Journal    
DOI: 10.1093/protein/8.8.801     Document Type: Article

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