Flexibility of human cytochrome P450 enzymes: Molecular dynamics and spectroscopy reveal important function-related variations

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1814, Issue 1, 2011, Pages 58-68

  Hendrychová, Tereza ^a   Anzenbacherová, Eva ^a   Hudeček, Jiří ^b   Skopalík, Josef ^a   Lange, Reinhard ^c   Hildebrandt, Peter ^d   Otyepka, Michal ^a   Anzenbacher, Pavel ^a  

^a PALACKÝ UNIVERSITY   (Czech Republic)

^b CHARLES UNIVERSITY   (Czech Republic)

^c UNIV MONTPELLIER   (France)

^d TECHNISCHE UNIVERSITÄT BERLIN   (Germany)

Author keywords

Cytochrome P450; Flexibility; Malleability; Molecular dynamics; Raman spectroscopy; UV VIS

Indexed keywords

CYTOCHROME P450 1A2; CYTOCHROME P450 2A6; CYTOCHROME P450 2C9; CYTOCHROME P450 2D6; CYTOCHROME P450 3A4; LIVER ENZYME;

ARTICLE; ENZYME ACTIVE SITE; ENZYME SPECIFICITY; HYPERBARISM; MOLECULAR DYNAMICS; MOLECULAR MODEL; PRIORITY JOURNAL; RAMAN SPECTROMETRY; ULTRAVIOLET SPECTROSCOPY;

ARYL HYDROCARBON HYDROXYLASES; CATALYTIC DOMAIN; CYTOCHROME P-450 CYP1A2; CYTOCHROME P-450 CYP2D6; CYTOCHROME P-450 CYP3A; CYTOCHROME P-450 ENZYME SYSTEM; HEME; HUMANS; HYDROSTATIC PRESSURE; ISOENZYMES; LIVER; MODELS, MOLECULAR; MOLECULAR DYNAMICS SIMULATION; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; SPECTROPHOTOMETRY; SPECTRUM ANALYSIS, RAMAN; SUBSTRATE SPECIFICITY;

EID: 78649444586     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2010.07.017     Document Type: Article

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