Intramolecular heme ligation of the cytochrome P450 2C9 R108H mutant demonstrates pronounced conformational flexibility of the B-C loop region: Implications for substrate binding

Biochemistry

Volumn 49, Issue 40, 2010, Pages 8700-8708

  Roberts, Arthur G ^a,d   Cheesman, Matthew J ^a   Primak, Andrew ^b   Bowman, Michael K ^c   Atkins, William M ^a   Rettie, Allan E ^a  

^a UNIVERSITY OF WASHINGTON   (United States)

^b SIEMENS CORPORATE RESEARCH   (United States)

^c UNIVERSITY OF ALABAMA   (United States)

^d UNIVERSITY OF CALIFORNIA SAN DIEGO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ABSORBANCE SPECTRUM; CONFORMATIONAL FLEXIBILITY; CYTOCHROME P450; HEME IRON; HEME LIGATION; IN-SILICO; LOOP REGIONS; MOLECULAR DYNAMICS SIMULATIONS; OPEN CONFORMATION; PULSED ELECTRON; SUBSTRATE BINDING; UV-VISIBLE; UV-VISIBLE ABSORBANCE SPECTROSCOPY;

AMINO ACIDS; ENZYMES; MOLECULAR DYNAMICS; MONOMERS; PARAMAGNETIC RESONANCE; PORPHYRINS; SIZE EXCLUSION CHROMATOGRAPHY;

CONFORMATIONS;

CYTOCHROME P450 2C9; HEME; HISTIDINE;

ARTICLE; CONFORMATIONAL TRANSITION; ELECTRON SPIN RESONANCE; ENZYME CONFORMATION; GEL PERMEATION CHROMATOGRAPHY; MOLECULAR DYNAMICS; MUTANT; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN STRUCTURE; SITE DIRECTED MUTAGENESIS;

ANIMALS; ARYL HYDROCARBON HYDROXYLASES; CHROMATOGRAPHY, GEL; ELECTRON SPIN RESONANCE SPECTROSCOPY; ESCHERICHIA COLI; HEME; HISTIDINE; HUMANS; MOLECULAR DYNAMICS SIMULATION; MUTANT PROTEINS; MUTATION; PROTEIN BINDING; PROTEIN CONFORMATION; RABBITS; SPECTROPHOTOMETRY, ULTRAVIOLET; SUBSTRATE SPECIFICITY;

ORYCTOLAGUS CUNICULUS;

EID: 77957682630     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi100911q     Document Type: Article

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