A structure-based model for cytochrome P450(cam)-putidaredoxin interactions

Biochimie

Volumn 78, Issue 8-9, 1996, Pages 723-733

  Pochapsky, T C ^a   Lyons, Ta ^a   Kazanis, S ^a   Arakaki, T ^a   Ratnaswamy, G ^a  

^a BRANDEIS UNIVERSITY   (United States)

Author keywords

Cytochrome P450; Electron transfer; Ferredoxin; Putidaredoxin; Redox proteins

Indexed keywords

ADRENODOXIN; CYTOCHROME P450; FERREDOXIN; NITROGEN 13; REDUCING AGENT;

ARTICLE; ELECTRON TRANSPORT; ENZYME KINETICS; ENZYME STRUCTURE; HYDROGEN BOND; ISOTOPE LABELING; MOLECULAR DYNAMICS; MOLECULAR MODEL; MUTAGENESIS; NUCLEAR MAGNETIC RESONANCE; PROTEIN PROTEIN INTERACTION; REDUCTION; STRUCTURE ACTIVITY RELATION;

EID: 0030457189     PISSN: 03009084     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0300-9084(97)82530-8     Document Type: Article

References (43)

1. 1 Baldwin JE, Morris GM, Richards WG (1991) Electron transport in cytochromes-P-450 by covalent switching. Proc R Soc Lond Ser B 245, 43-51
2. 2 Beckert V, Dettmer R, Bernhardt R (1994) Mutations of tyrosine 82 in bovine adrenodoxin that affect binding to cytochromes P45011A1 and P45011B1 but not electron transfer. J Biol Chem 269, 2568-2573
3. 3 Beckert V, Schrauber H, Bernhardt R, Van Dijk AA, Kakoschke C, Wray V (1995) Mutational effects on the spectroscopic properties and biological activities of oxidized bovine adrenodoxin, and their structural implications. Eur J Biochem 231, 226-235
4. 4 Bodenhausen G, Ruben DJ (1980) Natural abundance nitrogen-15 NMR by enhanced heteronuclear spectroscopy. Chem Phys Lett 69, 185-189
5. 5 Coghlan VM, Vickery LE (1991) Site-specific mutations in human ferredoxin that affect binding to ferredoxin reductase and cytochrome P40scc. J Biol Chem 266, 18606-18612
6. 6 Coghlan VM, Vickery LE (1992) Electrostatic interactions stabilizing ferredoxin electron transfer complexes. J Biol Chem 267, 8932-8935
7. 7 Cupp JR, Vickery LE (1989) Adrenodoxin with a COOH-terminal deletion (des 116-128) exhibits enhanced activity. J Biol Chem 264, 1602-1607
8. cam electron-transfer complex: Identification of the residue responsible for redox-state-dependent conformers. Biochemistry 31, 11383-11389
9. 9 Dugad LB, La Mar GN, Banci L, Bertini I (1990) Identification of localized redox states in plant-type two-iron ferredoxins using the nuclear Overhauser effect. Biochemistry 29, 2263-2271
10. 10 Geren L, Tuls J, O'Brien P, Millett F, Peterson JA (1986) The involvement of carboxylate groups of putidaredoxin in the reaction with putidaredoxin reductase. J Biol Chem 261, 15491-15495
11. cam methylene monooxygenase components: cytochrome m, putidaredoxin and putidaredoxin reductase. In: Methods Enzymol (Colowick SP, Kaplan NO, eds) New York, Academic Press, 52, 166-188
12. cam and putidaredoxin. J Biol Chem 257, 14324-14332
13. 13 Hintz MJ, Peterson JA (1981) The kinetics of reduction of cytochrome P-450cam by reduced putidaredoxin. J Biol Chem 256, 6721-6728
14. 14 Irie S, Doi S, Yorifuji T, Takagi M, Yano K (1987) Nucleotide sequencing and characterization of the genes encoding benzene oxidation enzymes of Pseudomonas putida. J Bacteriol 169, 5174-5179
15. 15 Kraulis PJ (1991) MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr 24, 946-950
16. cam. J Biol Chem 251, 1116-1124
17. 17 Lyons TA, Ratnaswamy G, Pochapsky TC (1996) Redox-dependent dynamics of putidaredoxin characterized by amide proton exchange. Protein Sci 5, 627-639
18. 18 McLendon G, Pardue K, Bak P (1987) Electron transfer in the cytochrome c/cytochrome b2 complex: Evidence for 'conformational gating'. J Am Chem Soc 109, 7540-7541
19. 19 Miura S, Ichikawa Y (1991) Conformational change of adrenodoxin induced by reduction of iron-sulfur cluster. Proton nuclear magnetic resonance study. J Biol Chem 266, 6252-6258
20. scc and adrenodoxin reductase. J Biol Chem 266, 19212-19216
21. cam research: Mechanistic insights into oxygenase catalysis. In: Cytochrome P450: Structure, Mechanism and Biochemistry (Ortiz de Montellano PR, ed) New York, Plenum Press, 83-124
22. cam in the electron transport from putidaredoxin. Biochim Biophys Acta 1207, 40-48
23. 23 Needleman SB, Wunsch CD (1970) A general method applicable to the search for similarities in the amino acid sequence of two proteins. J Mol Biol 48, 443-453
24. 24 Okamura T, John ME, Zuber MX, Simpson ER, Waterman MR (1985) Molecular cloning and amino acid sequence of the precursor form of bovine adrenodoxin: Evidence for a previously unidentified COOH-terminal peptide. Proc Natl Acad Sci USA 82, 5705-5709
25. 25 Pelletier H, Kraut J (1992) Crystal structure of a complex between electron transfer partners, cytochrome c peroxidase and cytochrome c. Science 258, 1749-1755
26. 26 Peterson JA, Lorence MC, Amarneh B (1990) Putidaredoxin reductase and putidaredoxin: Cloning, sequence determination, and heterologous expression of the proteins. J Biol Chem 265, 6066-6073
27. 27 Peterson JA, Lu JY, Geisselsoder J, Graham-Lorence S, Carmona C, Witney F, Lorence MC (1992) Cytochrome P-450terp. Isolation and purification of the protein and cloning and sequencing of its operon. J Biol Chem 267, 14193-14203
28. 28 Pochapsky TC, Gopen Q (1992) A chromatographic approach to the determination of relative free energies of interaction between hydrophobic and amphiphilic amino acid side chain. Protein Sci 1, 786-795
29. 29 Pochapsky TC, Ye XM, Ratnaswamy G, Lyons TA (1994) An NMR-derived model for the solution structure of oxidized putidaredoxin, a 2-Fe, 2-S ferredoxin from Pseudomonas. Biochemistry 33, 6424-6432
30. 1H NMR spectral features and tertiary structural constraints on the C-terminal region of putidaredoxin. Biochemistry 33, 6433-6441
31. 31 Poulos TL, Finzel BC, Howard AJ (1987) High resolution crystal structure of cytochrome P450cam. J Mol Biol 195, 687-700
32. cam ternary complex. Biochemistry 28, 7586-7592
33. 33 Shaka AJ, Barker PB, Freeman R (1985) Computer-optimized decoupling scheme for wideband applications and low-level operation. J Magn Reson 64, 547-552
34. 34 Sligar SG, Debrunner PG, Lipscomb JD, Namtvedt MJ, Gunsalus IC (1974) A role of the putidaredoxin COOH-terminus in P-450cam (cytochrome m) hydroxylations. Proc Natl Acad Sci USA 71, 3906-3910
35. 35 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
36. cam electron-transfer complex. Biochemistry 28, 8201-8205
37. 37 Stayton PS, Sligar SG (1990) The cytochrome P-450cam binding surface as defined by site-directed mutagenesis and electrostatic modeling. Biochemistry 29, 7381-7386
38. cam. Biochemistry 30, 1845-1851
39. 39 Xia B, Cheng H, Skjeldal L, Coghlan VM, Vickery LE, Markley JL (1995) Multinuclear magnetic resonance and mutagenesis studies of the histidine residues of human mitochondrial ferredoxin. Biochemistry 34, 180-187
40. 40 Wada A, Waterman, MR (1992) Identification by site-directed mutagenesis of two lysine residues in cholesterol side chain cleavage cytochrome P450 that are essential for adrenodoxin binding. J Biol Chem 267, 22877-22882
41. 41 Wagner G (1983) Characterization of the distribution of internal motions in the basic pancreatic trypsin inhibitor using a large number of internal NMR probes. Q Rev Biophysv 16, 1-57
42. 5 electron transfer complex. Science 238, 794-796
43. 43 Brewer CB, Peterson JA (1988) Single turnover kinetics of the reaction between oxycytochrome-P-450cam and reduced putidaredoxin. J Biol Chem 263, 791-798