Constrained water access to the active site of cytochrome P450 from the piezophilic bacterium Photobacterium profundum

High Pressure Research

Volumn 30, Issue 4, 2010, Pages 466-474

  Sineva, Elena V ^a   Davydov, Dmitri R ^a  

^a UNIVERSITY OF CALIFORNIA SAN DIEGO   (United States)

Author keywords

cytochrome P450; piezophilic organism; pressure perturbation spectroscopy; protein hydration; substrate binding

Indexed keywords

CYTOCHROME P450; PIEZOPHILIC ORGANISM; PRESSURE-PERTURBATION SPECTROSCOPY; PROTEIN HYDRATION; SUBSTRATE BINDING;

HYDRATION; HYDROSTATIC PRESSURE; PROTEINS; SUBSTRATES;

FATTY ACIDS;

EID: 78650318968     PISSN: 08957959     EISSN: 14772299     Source Type: Journal    
DOI: 10.1080/08957959.2010.535208     Document Type: Article

References (20)

1. D. H. Bartlett, Pressure effects on in vivo microbial processes, Biochim. Biophys. Acta 1595(2002), pp. 367-381.
2. G. Hui Bon Hoa, M. A. McLean, and S. G. Sligar, High pressure, a tool for exploring heme protein active sites, Biochim. Biophys. Acta 1595(2002), pp. 297-308.
3. D. Hamdane, H. Zhang, and P. Hollenberg, Oxygen activation by cytochrome P450 monooxygenase, Photosynth. Res. 98(2008), pp. 657-666.
4. F. Bancel, N. Bec, C. Ebel, and R. Lange, A central role for water in the control of the spin state of cytochrome P-450scc, Eur. J. Biochem. 250(1997), pp. 276-285.
5. A. Vezzi, S. Campanaro, M. D'Angelo, F. Simonato, N. Vitulo, F. M. Lauro, A. Cestaro, G. Malacrida, B. Simionati, N. Cannata, C. Romualdi, D. H. Bartlett, and G. Valle, Life at depth: Photobacterium profundum genome sequence and expression analysis, Science 307(2005), pp. 1459-1461.
6. D. R. Davydov, N. Y. Davydova, and J. R. Halpert, Allosteric transitions in cytochrome P450eryF explored with pressure-perturbation spectroscopy, lifetime FRET, and a novel fluorescent substrate, Fluorol-7GA, Biochemistry 47(2008), pp. 11348-11359.
7. G. Hui Bon Hoa, P. Douzou, N. Dahan, and C. Balny, High-pressure spectrometry at subzero temperatures, Anal. Biochem. 120(1982), pp. 125-135.
8. D. R. Davydov, E. Deprez, G. Hui Bon Hoa, T. V. Knyushko, G. P. Kuznetsova, Y. M. Koen and A. I. Archakov, High-pressure-induced transitions in microsomal cytochrome P450 2B4 in solution: Evidence for conformational inhomogeneity in the oligomers, Arch. Biochem. Biophys. 320(1995), pp. 330-344.
9. D. R. Davydov, G. Hui Bon Hoa, and J. A. Peterson, Dynamics of protein-bound water in the heme domain of P450BM3 studied by high-pressure spectroscopy: comparison with P450cam and P450 2B4, Biochemistry 38(1999), pp. 751-761.
10. G. Weber, Protein Interactions, Chapman & Hall, NewYork, 1991.
11. J. C. Talakad, P. R. Wilderman, D. R. Davydov, S. Kumar, and J. R. Halpert, Rational engineering of cytochromes P450 2B6 and 2B11 for enhanced stability: Insights into structural importance of residue 334, Arch. Biochem. Biophys. 494(2010), pp. 151-158.
12. C. Jung, G. Hui Bon Hoa, D. Davydov, E. Gill, and K. Heremans, Compressibility of the heme pocket of substrate analogue complexes of cytochrome P-450cam-CO. The effect of hydrostatic pressure on the Soret band, Eur J Biochem 233(1995), pp. 600-606.
13. W. Schwarze, J. Blanck, O. Ristau, G. R. Janig, K. Pommerening, H. Rein and K. Ruckpaul, Spin state control of cytochrome P-450 reduction and catalytic activity in a reconstituted P-450 LM2 system as induced by a series of benzphetamine analogues, Chem. Biol. Interact. 54(1985), pp. 127-141.
14. V. Helms, E. Deprez, E. Gill, C. Barret, G. Hui Bon Hoa, and R. C. Wade, Improved binding of cytochrome P450cam substrate analogues designed to fill extra space in the substrate binding pocket, Biochemistry 35(1996), pp. 1485-1499.
15. J. B. Schenkman, D. L. Cinti, S. Orrenius, P. Moldeus, and R. Kraschnitz, The nature of the reverse type I (modified type II) spectral change in liver microsomes, Biochemistry 11(1972), pp. 4243-4251.
16. T. Shimada, K. Tanaka, S. Takenaka, M. K. Foroozesh, N. Murayama, H. Yamazaki, F. P. Guengerich, and M. Komori, Reverse type I binding spectra of human cytochrome P450 1B1 induced by flavonoid, stilbene, pyrene, naphthalene, phenanthrene, and biphenyl derivatives that inhibit catalytic activity: A structure-function relationship study, Chem. Res. Toxicol. 22(2009), pp. 1325-1333.
17. V. Uvarov, V. E. Tretiakov, and A. I. Archakov, Heme maintains catalytically active structure of cytochrome P-450, FEBS Lett. 260(1990), pp. 309-312.
18. F. Bancel, G. Hui Bon Hoa, P. Anzenbacher, C. Balny, and R. Lange, High pressure: A new tool to study P450 structure and function, Methods Enzymol. 357(2002), pp. 145-157.
19. G. Hui Bon Hoa, M. A. McLean, and S. G. Sligar, High pressure, a tool for exploring heme protein active sites, Biochim. Biophys. Acta 1595(2002), pp. 297-308.
20. E. Anzenbacherova, N. Bec, P. Anzenbacher, J. Hudecek, P. Soucek, C. Jung, A. W. Munro, and R. Lange, Flexibility and stability of the structure of cytochromes P450 3A4 and BM-3, Eur. J. Biochem. 267(2000), pp. 2916-2920.