Mobility of norbornane-type substrates and water accessibility in cytochrome P-450(cam)

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1338, Issue 1, 1997, Pages 77-92

  Schulze, Heike ^a   Hoa, Gaston Hui Bon ^b   Jung, Christiane ^a  

^a MAX DELBRÜCK CENTER FOR MOLECULAR MEDICINE   (Germany)

^b INST DE BIOLOGIE PHYSICO CHIMIQUE   (France)

Author keywords

Conformation and dynamics; Cytochrome P 450(cam); Enzyme substrate interaction; Solvent effect; UV Vis spectroscopy, low temperature high pressure

Indexed keywords

CAMPHOR; CYTOCHROME P450; NORBORNANE DERIVATIVE;

ABSORPTION SPECTROSCOPY; ARTICLE; ENZYME CONFORMATION; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; PH; PRESSURE; PRIORITY JOURNAL; SOLVATION; TEMPERATURE;

BINDING SITES; CALORIMETRY; CAMPHOR; CAMPHOR 5-MONOOXYGENASE; CLONING, MOLECULAR; ESCHERICHIA COLI; HYDROGEN-ION CONCENTRATION; KINETICS; MOLECULAR STRUCTURE; NORBORNANES; PRESSURE; PSEUDOMONAS PUTIDA; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY; THERMODYNAMICS;

DRYOBALANOPS;

EID: 0342617660     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(96)00192-6     Document Type: Article

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