Role of substrate on the conformational stability of the heme active site of cytochrome P450cam: Effect of temperature and low concentrations of denaturants

Journal of Biological Inorganic Chemistry

Volumn 9, Issue 4, 2004, Pages 477-488

  Murugan, R ^a   Mazumdar, Shyamalava ^a  

^a TATA INSTITUTE OF FUNDAMENTAL RESEARCH   (India)

Author keywords

Conformational stability; Cytochrome P450cam; Heme; Spectral deconvolution; Tertiary structure

Indexed keywords

CAMPHOR; CYTOCHROME P450; HEME;

ARTICLE; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN TERTIARY STRUCTURE; TEMPERATURE; TEMPERATURE DEPENDENCE; THERMODYNAMICS; ULTRAVIOLET RADIATION;

BINDING SITES; CAMPHOR; CAMPHOR 5-MONOOXYGENASE; HEMEPROTEINS; LIGANDS; PROTEIN CONFORMATION; PROTEIN DENATURATION; SPECTRUM ANALYSIS; TEMPERATURE; THERMODYNAMICS;

DRYOBALANOPS;

EID: 3042755600     PISSN: 09498257     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00775-004-0544-1     Document Type: Article

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