Substrates modulate the rate-determining step for CO binding in cytochrome P450cam (CYP101): A high-pressure stopped-flow study

European Journal of Biochemistry

Volumn 269, Issue 12, 2002, Pages 2989-2996

  Jung, Christiane ^a   Bec, Nicole ^b   Lange, Reinhard ^b  

^a MAX DELBRÜCK CENTER FOR MOLECULAR MEDICINE   (Germany)

^b INSERM   (France)

Author keywords

CO ligand binding; Cytochrome P450; High pressure stopped flow; Protein dynamics

Indexed keywords

CAMPHOR 5 MONOOXYGENASE; CAMPHOR DERIVATIVE; CARBON MONOXIDE; WATER;

ARTICLE; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME SUBSTRATE COMPLEX; FLOW RATE; NONHUMAN; PHOTOLYSIS; PRIORITY JOURNAL; STEADY STATE;

BINDING SITES; BORNANES; CAMPHOR; CAMPHOR 5-MONOOXYGENASE; CARBON MONOXIDE; KINETICS; NORBORNANES; PSEUDOMONAS PUTIDA; SUBSTRATE SPECIFICITY;

DRYOBALANOPS;

EID: 0036314910     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2002.02980.x     Document Type: Article

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