Linking of cytochrome P450cam and putidaredoxin by a co-ordination bridge

Biocatalysis and Biotransformation

Volumn 25, Issue 2-4, 2007, Pages 301-317

  Rojubally, Adina ^a   Cheng, Shu Hua ^b   Foreman, Christie ^a   Huang, Jian ^a   Agnes, George R ^a   Plettner, Erika ^a  

^a SIMON FRASER UNIVERSITY   (Canada)

^b NATIONAL CHI NAN UNIVERSITY   (Taiwan)

Author keywords

Chemical modification; Coupling; Cytochrome P450; Ferredoxin; Hydroxylation; Peptide mapping

Indexed keywords

C-TERMINUS; CYTOCHROME P450; DIOXYGENS; PEPTIDE MAPPING; PUTIDAREDOXIN; REDUCTANTS; SINGLE PRODUCT; STRONG BINDING; TRANSFER ELECTRONS;

CAMS; HYDROXYLATION; OXIDATION; PEPTIDES; PHOSPHATASES;

CHEMICAL MODIFICATION;

EID: 35348900302     PISSN: 10242422     EISSN: 10292446     Source Type: Journal    
DOI: 10.1080/10242420701422799     Document Type: Article

References (53)

1. Atkins WM, Sligar SG. 1987. Metabolic switching in cytochrome P450cam: deuterium isotope effects on regiospecificity and the monooxygenase/oxidase ratio. J Am Chem Soc 109:3754-3760.
2. Atkins WM, Sligar SG. 1988. Deuterium isotope effects in norcamphor metabolism by cytochrome P450cam: Kinetic evidence for the two-electron reduction of a high-valent ironoxo intermediate. Biochemistry 27:1610-1616.
3. Bell SG, Chen X, Swoden RJ, Xu F, Williams JN,Wong L-L, Rao ZH. 2003. Molecular recognition in (+)-α-pinene oxidation by cyctochrome P450cam. J Am Chem Soc 125:705-708. (Pubitemid 36109932)
4. Collman JP, Chien AS, Eberspacher TA, Brauman JI. 1998. An agostic alternative to the P-450 rebound mechanism. J Am Chem Soc 120:425-426.
5. Davies MD, Sligar SG. 1992. Genetic variants in the putidaredoxin- cytochrome P-450cam electron-transfer complex: Identification of the residue responsible for redox-state-dependent conformers. Biochemistry 31:11383-11389.
6. Davydov R, Makris TM, Kofman V, Werst DE, Sligar SG, Hoffman BM. 2001. Hydroxylation of camphor by reduced oxy-cytochrome P450cam: Mechanistic implications of EPR and ENDOR studies of catalytic intermediated in native and mutant enzymes. J Am Chem Soc 123:1403-1415. (Pubitemid 32167333)
7. Deprez E, Gerber NC, Primo CD, Douzou P, Sligar SG, Hoa GHB. 1994. Electrostatic control of the substrate access channel in cytochrome P-450cam. Biochemistry 33:14464-14468
8. Dunn AR, Dmochowski IJ, Winkler JR, Gray HB. 2003. Nanosecond photoreduction of cytochrome P450cam by channel-specific Ru-diimine electron tunneling wires. J Am Chem Soc 125:12450-12456.
9. England PA, Harford-Cross CF, Stevenson JA, Rouch DA, Wong L-L. 1998. The oxidation of naphthalene and pyrene by cytochrome P450cam. FEBS Lett 424:271-274.
10. Fisher MT, Sligar SG. 1985. Control of heme protein redox potential and reduction rate: Linear free energy relation between potential and ferric spin state equilibrium. J Am Chem Soc 107:5018-5019.
11. Furukawa Y, Morishima I. 2001. The role of water molecules in the association of cytochrome P450cam with putidaredoxin. J Biol Chem 276:12983-12990.
12. Gelb MH, Heimbrook DC, Malkonene P, Sligar SG. 1982. Stereochemistry and deuterium isotope effects in camphor hydroxylation by the cytochrome P450cam monooxygenase system. Biochemistry 21:370-377.
13. Gould PV, Gelb MH, Sligar SG. 1981. Interaction of 5-bromocamphor with cytochrome P450cam. J Biol Chem 256:6686-6691.
14. Gunsalus IC, Wagner GC. 1978. Bacterial P-450cam methylene monooxygenase components: Cytochrome m, putidaredoxin, and putidaredoxin reductase. Methods Enzymol 52C:166-188.
15. Hildebrandt AG, Roots I. 1975. Reduced nicotinamide adenine dinucleotide phosphate (NADPH)-dependent formation and breakdown of hydrogen peroxide during mixed function oxidation reactions in liver microsomes. Arch Biochem Biophys 171:385-397.
16. Hlavica P, Schulze J, Lewis DFV. 2003. Functional interaction of cytochrome P450 with its redox partners: A critical assessment and update of the topology of predicted contact regions. J Inorg Biochem 96:279-297. (Pubitemid 36900366)
17. Holden M, Mayhew M, Bunk D, Roitberg A, Vilker V. 1997. Probing the interactions of putidaredoxin with redox partners in camphor P450 5-monooxygenase by mutagenesis of surface residues. J Biol Chem 272:21720-21725. (Pubitemid 27382785)
18. cam enzyme system. FEBS Lett 451:351-353.
19. Kadkhodayan S, Coulter ED, Maryniak DM, Bryson TA, Dawson JH. 1995. Uncoupling oxygen transfer and electron transfer in the oxygenation of camphor analogues by cytochrome P450-CAM. J Biol Chem 270:28042-28048.
20. Kamachi T, Yoshizawa K. 2003. A theoretical study on the mechanism of camphor hydroxylation by compound I of cytochrome P450. J Am Chem Soc 125:4652-4661. (Pubitemid 36418711)
21. Kumar D, de Visser SP, Shaik S. 2003. How does product isotope effect prove the operation of a two-state 'rebound' mechanism in C-H hydroxylation by cytochrome P450? J Am Chem Soc 125:13024-13025.
22. Lipscomb JD, Sligar SG, Namtvedt MJ, Gunsalus IC. 1976. Autooxidation and hydroxylation reactions of oxygenated cytochrome P450cam. J Biol Chem 251:1116-1124.
23. Loida PJ, Sligar SG. 1994. Molecular recognition in cytochrome P450: control of uncoupling reactions via site-directed mutagenesis. In: Lechner MC, editor. Cytochrome P450. Eighth International Conference. Paris: John Libbey Eurotext. p 463-466.
24. Manchester JI, Dinnocenzo JP, Higgins LH, Jones JP. 1997. A new mechanistic probe for cytochrome P450: An application of isotope effect profiles. J Am Chem Soc 119:5069-5070.
25. Mayer JM. 2000. Thermodynamic influences on C-H bond oxidation. In: Maerrnier B, editor. Biomimetic ox. catalyzed by TM complexes. London: Imperial College Press. p 1-37.
26. Meer BW, Coker G III, Chen S-YS. 1994. Resonance energy transfer, theory and data. Weinheim: VCH.
27. Newcomb M, Tadic-Biadatti M-HL, Chestney DL, Roberts ES, Hollenberg PF. 1995. A nonsynchronous concerted mechanism for cytochrome P-450 catalyzed hydroxylation. J Am Chem Soc 117:12085-12091. (Pubitemid 3015876)
28. Nickerson DP, Harford-Cross CF, Fulcher SR, Wong L-L. 1997. The catalytic activity of cytochrome P450cam towards styrene oxidation is increased by site-specific mutagenesis. FEBS Lett 405:153-156.
29. O'Keeffe DH, Ebel RE, Peterson JA. 1978. Purification of bacterial cytochrome P-450. Methods Enzymol 52C:151-156.
30. Ogliaro F, Cohen S, de Visser SP, Shaik S.. 2000. Medium polarization and hydrogen bonding effects on compound I of cytochrome P450: What kind of a radical is it really? J Am Chem Soc 122:12892-12893.
31. Ortiz de Montellano P, editor. (1995) Cytochrome P450. Structure, mechanism and biochemistry (second ed.), New York: Plenum Press.
32. Peterson JA. 1971. Camphor binding by Pseudomonas putida cytochrome P-450. Arch Biochem Biophys 144:678-693.
33. Plettner E, DeSantis G, Stabile M, Jones JB. 1999. Modulation of esterase and amidase activity of subtilisin Bacillus lentus by chemical modification of cysteine mutants. J Am Chem Soc 121:4977-4981. (Pubitemid 129541017)
34. Pochapsky TC, Ratnaswamy G, Patera A. 1994. Redox-dependent 1H NMR spectral features and tertiary structural constraints on the C-terminal region of putidaredoxin. Biochemistry 33:6433-6441. (Pubitemid 2096758)
35. cam-putidaredoxin couple. Biochemistry 42:5649-5656.
36. Poulos TL, Finzel BC, Howard AJ. 1986. Crystal structure of substrate-free Pseudomonas putida cytochrome P-450. Biochemistry 25:5314-5322.
37. cam. J Mol Biol 195:687-700.
38. Reipa V, Mayhew MP, Vilker VL. 1997. A direct electrode-driven P450 cycle for biocatalysis. Proc Natl Acad Sci USA 94:13554-13558. (Pubitemid 28009621)
39. cam. Theory and experiments. J Am Chem Soc 120:8927-8932.
40. cam at atomic resolution. Science 287:1615-1622.
41. Shimada H, Nagano S, Ariga Y, Unno M, Egawa T, Hishiki T, Ishimura Y. 1999. Putidaredoxin-cytochrome P450cam interaction. Spin state of the heme iron modulates putidaredoxin structure. J Biol Chem 274:9363-9369. (Pubitemid 129517905)
42. Sibbesen O, DeVoss JJ, Ortiz de Montellano PR. 1996. Putidaredoxin reductase-putidaredoxin-cytochrome P450cam triple fusion protein. J Biol Chem 271:22462-22469.
43. Sibbesen O, Zhang ZP, Montellano PROd. 1998. Cytochrome P450cam substrate specificity: Relationship between structure and catalytic oxidation of alkylbenzenes. Arch Biochem Biophys 353:285-296. (Pubitemid 28373013)
44. Sligar SG. 1976. Coupling of spin, substrate, and redox equilibria in cytochrome P450. Biochemistry 15:5399-5406.
45. Sligar SG, Gunsalus IC. 1976. A thermodynamic model of regulation: Modulation of redox equilibria in camphor monoxygenase. Proc Natl Acad Sci USA 73:1078-1082.
46. cam (cytochrome m*) hydroxylations. Proc Natl Acad Sci USA 71:3906-3910.
47. Sono M, Roach MP, Coulter ED, Dawson JH. 1996. Hemecontaining oxygenases. Chem Rev 96:2841-2887.
48. Taraphder S, Hummer G. 2003. Protein side-chain motion and hydration in proton-transfer pathways. Results for cytochrome P450cam. J Am Chem Soc 125:3931-3940. (Pubitemid 36512385)
49. cam-putidaredoxin: Roles of glutamine 360 at the heme proximal site. Biochemistry 41:13883-13893.
50. Toy PH, Newcomb M, Hollenberg PF. 1998. Hypersensitive mechanistic probe studies of cytochrome P450-catalyzed hydroxylation reactions. Implications for the cationic pathway. J Am Chem Soc 120:7719-7729. (Pubitemid 28392053)
51. Wilker JJ, Dmochowski IJ, Dawson JH, Winkler JR, Gray HB. 1999. Substrates for rapid delivery of electrons and holes to buried active sites in proteins. Agnew Chem Int Ed 38:89-92.
52. Woggon W-D. 1996. Topics in current chemistry. Berlin: Springer-Werlag Berlin Heidelberg. p 40-93.
53. Wong L-L. 1998. Cytochrome P450 monooxygenases. Curr Opin Chem Biol 2:263-268.