Carbon monoxide binding to cytochrome P450(BM-3): Evidence for a substrate-dependent conformational change

Biochimie

Volumn 78, Issue 8-9, 1996, Pages 700-705

  McLean, M A ^a   Yeom, H ^a   Sligar, S G ^a  

^a UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

Author keywords

Carbon monoxide binding; Hemoprotein; P450(BM 3)

Indexed keywords

CARBON MONOXIDE; CYTOCHROME P450; LAURIC ACID;

ARTICLE; CONFORMATIONAL TRANSITION; ENERGY; ENZYME KINETICS; ENZYME SUBSTRATE COMPLEX; MODEL; PHOTOLYSIS;

EID: 0030458846     PISSN: 03009084     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0300-9084(97)82527-8     Document Type: Article

References (19)

1. 1 Austin RH, Beeson KW, Eisenstein L, Frauenfelder H, Gunsalus IC (1975) Dynamics of ligand binding to myoglobin. Biochemistry 14, 5355-5373
2. 2 Doster W, Beece D, Bowne SF, Dilorio EE, Eisenstein L, Frauenfelder H, Reinisch L, Shyamsunder E, Winterhalter KH, Yue KT (1982) Control and pH dependence of ligand binding to heme proteins. Biochemistry 21, 4831-1839
3. 3 Kato M, Makino R, Iizuka T (1995) Thermodynamic aspects of the CO-binding reaction to P-450cam. Relevance with their biological significance and structure. Biochim Biophys Acta 1246, 178-184
4. 4 Alben JO, Beece D, Bowne SF, Doster W, Eisenstein L, Frauenfelder H, Good D, McDonald JD, Marden MC, Moh PP, Reinisch L, Reynolds AH, Shyamsunder E, Yue KT (1982) Infrared spectroscopy of photo-dissociated carboxymyoglobin at low temperatures. Proc Natl Acad Sci USA 79, 3744-3748
5. 5 Frauenfelder H, Petsko GA, Tsernoglu D (1979) Temperature dependent X-ray diffraction as a probe of protein structural dynamics. Nature (Lond) 280, 558-563
6. 6 Springer BA, Sligar SG, Olson JS, Phillips GN (1994) Mechanisms of ligand recognition in myglobin. Chem Rev 94, 699-714
7. 7 Peterson JA, Griffin BW (1972) Carbon monoxide binding by Pseudomonas putida cytochrome P-450. Arch Biochem Biophys 151, 427-433
8. 8 O' Keefe DH, Ebel RE, Peterson JA, Maxwell JC, Caughey WS (1978) An infrared spectroscopic study of CO bonding to ferrous cytchrome P-450. Biochemistry 17, 5845-5852
9. CAM ternary complex. Biochemistry 28, 7586-7592
10. 10 Unno M, Ishimori K, Ishimura Y, Morishima I (1994) High-pressure flash photolysis study of hemoprotein: Effects of substrate analogues on the recombination of carbon monoxide to cytochrome P450cam. Biochemistry 33, 9762-9768
11. 11 Tian WD, Wells AV, Champion PM, DiPrimo C, Gerber N, Sugar SG (1995) Measurements of CO geminate recombination in cytochromes P450 and P420. J Biol Chem 270, 8673-8679
12. 12 Wen LF, Fulco AJ (1987) Cloning of the gene encoding a catalytically self-sufficient cytochrome P-450 fatty acid monooxygenase induced by barbiturates in Bacillus megaterium and its functional expression and regulation in heterologous (Escherichia coli) and homologous (Bacillus megaterium) hosts. J Biol Chem 262, 6676-6682
13. 13 Sevrioukova IF, Peterson JA (1995) Reaction of carbon monoxide and molecular oxygen with P450terp (CYP108) and P450BM-3 (CYP102). Arch Biochem Biophys 317, 397-404
14. 14 Yeom H, Sligar SG, Li H, Poulos TL, Fulco AJ (1995) The role of Thr268 in oxygen activation of cytochrome P450BM-3. Biochemistry 34, 14733-14740
15. 15 Carsill RW (1990) Carbon Monoxide. Pergamon Press
16. 16 Ravichandran KG, Bouddupalli SS, Hasemann CA, Peterson JA, Deisenhofer J (1993) Crystal structure of hemoprotein domain of P450BM-3, a prototype for microsomal P450's. Science 261, 731-736
17. 17 Paulsen MD, Ornstein RL (1995) Dramatic differences in the motions of the mouth of open and closed cytochrome P-450BM-3 by molecular dynamics simulations. Proteins 21, 237-243
18. 18 Jung C, Hui Bon Hoa G, Schroder KL, Simon M, Doucet JP (1992) Substrate analogue induced changes of the CO-stretching mode in the cytochrome P450cam-carbon monoxide complex. Biochemistry 31, 12855-12862
19. cam. Biochemistry 34, 8982-8988