Functional role of residues in the helix B′ region of cytochrome P450 2B1

• Published in: Archives of biochemistry and biophysics Vol. 435; no. 1; pp. 157 - 165
• Main Authors: Honma, Wataru, Li, Weihua, Liu, Hong, Scott, Emily E., Halpert, James R.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.03.2005
• Subjects: Amino Acid Substitution; Amino Acids - chemistry; Amino Acids - genetics; Amino Acids - metabolism; Binding Sites; Cytochrome P-450 CYP2B1 - chemistry; Cytochrome P-450 CYP2B1 - genetics; Cytochrome P-450 CYP2B1 - metabolism; Cytochrome P450; Models, Chemical; Models, Molecular; Monooxygenase; Protein Binding; Protein Conformation; Protein Structure, Secondary; Recombinant Proteins - chemistry; Site-directed mutagenesis; Structure-Activity Relationship; Testosterone - chemistry; Testosterone - metabolism; Monooxygenase; Cytochrome P450; Site-directed mutagenesis

Comparison of several recently determined X-ray crystal structures of mammalian cytochrome P450 family 2 enzymes suggests considerable movement of helix B′ when ligands bind. To investigate the functional role of helix B′ in P450 2B1, residues 100–109 were substituted with alanine and phenylalanine....