Water Oxidation by a Cytochrome P450: Mechanism and Function of the Reaction

PLoS ONE

Volumn 8, Issue 4, 2013, Pages

  Prasad, Brinda ^a   Mah, Derrick J ^a   Lewis, Andrew R ^a   Plettner, Erika ^a  

^a SIMON FRASER UNIVERSITY   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

BORNEOL; CAMPHOR; CYTOCHROME P450; CYTOCHROME P450 101A1; HYDROGEN PEROXIDE; UNCLASSIFIED DRUG; BORNANE DERIVATIVE; ISOBORNEOL; WATER;

ARTICLE; CATALYSIS; COMPLEX FORMATION; CONTROLLED STUDY; DEUTERON NUCLEAR MAGNETIC RESONANCE; DOWN REGULATION; ELECTRON TRANSPORT; ENZYME KINETICS; ENZYME MECHANISM; HYDROGEN BOND; MICHAELIS MENTEN KINETICS; NUCLEOTIDE SEQUENCE; OXIDATION REDUCTION REACTION; OXYGEN CONCENTRATION; PH; PROTEIN EXPRESSION; PROTON NUCLEAR MAGNETIC RESONANCE; BIOMECHANICS; CHEMICAL STRUCTURE; CHEMISTRY; GENE EXPRESSION REGULATION; METABOLISM; PROTEIN CONFORMATION;

BACTERIA (MICROORGANISMS); DRYOBALANOPS;

BIOMECHANICAL PHENOMENA; BORNANES; CAMPHOR; CYTOCHROME P-450 ENZYME SYSTEM; GENE EXPRESSION REGULATION, ENZYMOLOGIC; HYDROGEN PEROXIDE; MODELS, MOLECULAR; OXIDATION-REDUCTION; PROTEIN CONFORMATION; WATER;

EID: 84876728072     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0061897     Document Type: Article

References (41)

1. De Montellano PRO (1995) Cytochrome P450 Structure, Mechanism and Biochemistry. Structural studies on prokaryotic P450s Second edition.
2. Schlichting I, Berendzen J, Chu K, Stock AM, Maves SA, et al. (2000) The catalytic pathway of cytochrome P450cam at atomic resolution. Science 287: 1615-1622.
3. Sligar SG, Gunsalus IC, (1976) A thermodynamic model of regulation: modulation of redox equilibria in camphor monoxygenase. Proc Natl Acad Sci U S A 73: 1078-1082.
4. Glascock MC, Ballou DP, Dawson JH, (2005) Direct observation of a novel perturbed oxyferrous catalytic intermediate during reduced putidaredoxin-initiated turnover of cytochrome P450cam- Probing the effector role of putidaredoxin in catalysis. J Biol Chem 280: 42134-42141.
5. Tanaka M, Haniu M, Yasunobu KT, Dus K, Gunsalus IC, (1974) Amino-Acid Sequence of Putidaredoxin, an Iron-Sulfur Protein from Pseudomonas putida. J Biol Chem 249: 3689-3701.
6. Cho KB, Hirao H, Chen H, Carvajal MA, Cohen S, et al. (2008) Compound I in heme thiolate enzymes: a comparative QM/MM study. J Phys Chem A 112: 13128-13138.
7. Chefson A, Auclair K, (2006) Progress towards the easier use of P450 enzymes. Mol Biosyst 2: 462-469.
8. Chefson A, Zhao J, Auclair K, (2006) Replacement of natural cofactors by selected hydrogen peroxide donors or organic peroxides results in improved activity for CYP3A4 and CYP2D6. Chembiochem 7: 916-919.
9. Auclair K, Moenne-Loccoz P, de Montellano PRO, (2001) Roles of the proximal heme thiolate ligand in cytochrome P450cam. J Am Chem Soc 123: 4877-4885.
10. Gunsalus IC, Wagner GC, (1978) Bacterial P450cam methylene monooxygenase components: cytochrome m, putidaredoxin, and putidaredoxin reductase. Methods Enzymol 52: 166-188.
11. Poulos TL, Finzel BC, Howard AJ, (1987) High-resolution crystal structure of cytochrome P450cam. J Mol Biol 195: 687-700.
12. Harada K, Sakurai K, Ikemura K, Ogura T, Hirota S, et al. (2008) Evaluation of the functional role of the heme-6-propionate side chain in cytochrome P450cam. J Am Chem Soc 130: 432-433.
13. Dau H, Limberg C, Reier T, Risch M, Roggan S, et al. (2010) The Mechanism of Water Oxidation: From Electrolysis via Homogeneous to Biological Catalysis. Chemcatchem 2: 724-761.
14. Izgorodin A, Winther-Jensen O, MacFarlane DR, (2012) On the Stability of Water Oxidation Catalysts: Challenges and Prospects. Aust J Chem 65: 638-642.
15. Zhou FL, Izgorodin A, Hocking RK, Spiccia L, MacFarlane DR, (2012) Electrodeposited MnOx Films from Ionic Liquid for Electrocatalytic Water Oxidation. Advanced Energy Materials 2: 1013-1021.
16. Prasad B, Rojubally A, Plettner E, (2011) Identification of Camphor Oxidation and Reduction Products in Pseudomonas putida: New Activity of the Cytochrome P450cam System. J Chem Ecol 37: 657-667.
17. Rojubally A, Hua Cheng S, Foreman C, Huang J, Agnes G, et al. (2007) Linking of cytochrome P450cam and putidaredoxin by a co-ordination bridge. Biocatalysis and Biotransformation 25: 301-317.
18. Rojubally A (2007) Linking Cytochrome P450cam to its Redox partner Putidaredoxin and probing new reactions of the Cytochrome P450cam system. PhD Thesis, Simon Fraser University.
19. Prasad B, Lewis AR, Plettner E, (2011) Enrichment of H217O from tap water, characterization of the enriched water, and properties of several 17O-labeled compounds. Anal Chem 83: 231-239.
20. Casny M, Rehder D, Schmidt H, Vilter H, Conte V, (2000) A 17O NMR study of peroxide binding to the active centre of bromoperoxidase from Ascophyllum nodosum. J Inorg Biochem 80: 157-160.
21. Cha Y, Murray CJ, Klinman JP, (1989) Hydrogen tunneling in enzyme reactions. Science 243: 1325-1330.
22. Huskey WP, Schowen RL, (1983) Reaction-Coordinate Tunneling in Hydride-Transfer Reactions. J Am Chem Soc 105: 5704-5706.
23. Nagel ZD, Klinman JP, (2006) Tunneling and dynamics in enzymatic hydride transfer. Chemical Reviews 106: 3095-3118.
24. Koppenol WH, Liebman JF, (1984) The Oxidizing Nature of the Hydroxyl Radical- a Comparison with the Ferryl Ion (FeO2+). J Phys Chem 88: 99-101.
25. Green MT, Dawson JH, Gray HB, (2004) Oxoiron(IV) in chloroperoxidase compound II is basic: implications for P450 chemistry. Science 304: 1653-1656.
26. Hishiki T, Shimada H, Nagano S, Egawa T, Kanamori Y, et al. (2000) X-ray crystal structure and catalytic properties of Thr252Ile mutant of cytochrome P450cam: roles of Thr252 and water in the active center. J Biochem 128: 965-974.
27. Wardman P, (1989) Reduction Potentials of One-Electron Couples Involving Free-Radicals in Aqueous-Solution. J Phys Chem Ref Data 18: 1637-1755.
28. Schlichting I, Berendzen J, Chu K, Stock AM, Maves SA, et al. (2000) The catalytic pathway of cytochrome P450cam at atomic resolution. Science 287: 1615-1622.
29. Yano JK, Wester MR, Schoch GA, Griffin KJ, Stout CD, et al. (2004) The structure of human microsomal cytochrome P450 3A4 determined by X-ray crystallography to 2.05-A resolution. J Biol Chem 279: 38091-38094.
30. Amunom I, Dieter LJ, Tamasi V, Cai J, Conklin DJ, et al. (2011) Cytochromes P450 catalyze the reduction of alpha,beta-unsaturated aldehydes. Chem Res Toxicol 24: 1223-1230.
31. Kaspera R, Sahele T, Lakatos K, Totah RA, (2012) Cytochrome P450BM-3 reduces aldehydes to alcohols through a direct hydride transfer. Biochem Biophys Res Commun 418: 464-468.
32. Cooper HL, Groves JT, (2011) Molecular probes of the mechanism of cytochrome P450. Oxygen traps a substrate radical intermediate. Arch Biochem Biophys 507: 111-118.
33. Hlavica P, Lewis DF, (2001) Allosteric phenomena in cytochrome P450-catalyzed monooxygenations. Eur J Biochem 268: 4817-4832.
34. Song WJ, Gucinski G, Sazinsky MH, Lippard SJ, (2011) Tracking a defined route for O2 migration in a dioxygen-activating diiron enzyme. Proc Natl Acad Sci U S A 108: 14795-14800.
35. Kallio JP, Rouvinen J, Kruus K, Hakulinen N, (2011) Probing the dioxygen route in Melanocarpus albomyces laccase with pressurized xenon gas. Biochemistry 50: 4396-4398.
36. Johnson BJ, Cohen J, Welford RW, Pearson AR, Schulten K, et al. (2007) Exploring molecular oxygen pathways in Hansenula polymorpha copper-containing amine oxidase. J Biol Chem 282: 17767-17776.
37. Wade RC, Winn PJ, Schlichting I, (2004) Sudarko (2004) A survey of active site access channels in cytochromes P450. J Inorg Biochem 98: 1175-1182.
38. Petrek M, Kosinova P, Koca J, Otyepka M, (2007) MOLE: a Voronoi diagram-based explorer of molecular channels, pores, and tunnels. Structure 15: 1357-1363.
39. Cryle MJ, Stok JE, De Voss JJ, (2003) Reactions catalyzed by bacterial cytochromes P450. Aust J Chem 56: 749-762.
40. Gunsalus IC, Sligar SG, (1976) Redox regulation of cytochrome P450cam mixed function oxidation by putidaredoxin and camphor ligation. Biochimie 58: 143-147.
41. Taylor DG, Trudgill PW, (1986) Camphor revisited: studies of 2,5-diketocamphane 1,2-monooxygenase from Pseudomonas putida ATCC 17453. J Bacteriol 165: 489-497.