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

References

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