P450bm 3 - A Model for Eukaryotic P450

Peterson, Julian A.

Abstract

Funding Agency

• Agency: National Institute of Health (NIH)
• Institute: National Institute of General Medical Sciences (NIGMS)
• Type: Research Project (R01)
• Project #: 5R01GM050858-03
• Application #: 2188994
• Study Section: Physical Biochemistry Study Section (PB)
• Project Start: 1994-08-01
• Project End: 1998-07-31
• Budget Start: 1996-08-01
• Budget End: 1997-07-31
• Support Year: 3
• Fiscal Year: 1996

Institution

• Name: University of Texas Sw Medical Center Dallas
• Department: Biochemistry
• Type: Schools of Medicine
• City: Dallas
• State: TX
• Country: United States
• Zip Code: 75390

Publications

Davydov, Dmitri R; Ponomarev, Gelii V; Bobrovnikova-Marjon, Ekaterina et al. (2013) Aluminum-substituted heme domain of P450BM-3 (BMP): introducing a heme-derived fluorescent probe for studies of substrate binding and protein-protein interactions in cytochromes P450. Biotechnol Appl Biochem 60:41-51

Haines, Donovan C; Hegde, Amita; Chen, Baozhi et al. (2011) A single active-site mutation of P450BM-3 dramatically enhances substrate binding and rate of product formation. Biochemistry 50:8333-41

Haines, Donovan C; Chen, Baozhi; Tomchick, Diana R et al. (2008) Crystal structure of inhibitor-bound P450BM-3 reveals open conformation of substrate access channel. Biochemistry 47:3662-70

Kitazume, Tatsuya; Haines, Donovan C; Estabrook, Ronald W et al. (2007) Obligatory intermolecular electron-transfer from FAD to FMN in dimeric P450BM-3. Biochemistry 46:11892-901

Hegde, Amita; Haines, Donovan C; Bondlela, Muralidhar et al. (2007) Interactions of substrates at the surface of P450s can greatly enhance substrate potency. Biochemistry 46:14010-7

Conley, Alan; Mapes, Samantha; Corbin, C Jo et al. (2002) Structural determinants of aromatase cytochrome p450 inhibition in substrate recognition site-1. Mol Endocrinol 16:1456-68

Kariakin, Andrei; Davydov, Dimitri; Peterson, Julian A et al. (2002) A new approach to the study of protein-protein interaction by FTIR: complex formation between cytochrome P450BM-3 heme domain and FMN reductase domain. Biochemistry 41:13514-25

Graham, Sandra E; Peterson, Julian A (2002) Sequence alignments, variabilities, and vagaries. Methods Enzymol 357:15-28

Usanov, Sergey A; Graham, Sandra E; Lepesheva, Galina I et al. (2002) Probing the interaction of bovine cytochrome P450scc (CYP11A1) with adrenodoxin: evaluating site-directed mutations by molecular modeling. Biochemistry 41:8310-20

Conley, A; Mapes, S; Corbin, C J et al. (2001) A comparative approach to structure-function studies of mammalian aromatases. J Steroid Biochem Mol Biol 79:289-97