Relocation of the distal histidine in cytochrome c peroxidase: Properties of CcP(W51H), CcP(W51H/H52W), and CcP(W51H/H52L)

Biochemistry

Volumn 48, Issue 23, 2009, Pages 5417-5425

  Foshay, Miriam C ^a   Vitello, Lidia B ^a   Erman, James E ^a  

^a NORTHERN ILLINOIS UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ASSOCIATION RATE CONSTANTS; COMPOUND I; CYTOCHROME C; DISSOCIATION RATE CONSTANT; DISTAL HISTIDINE; ELECTRONIC ABSORPTION SPECTRA; HEME GROUP; HEME IRON; HEME PROTEINS; HISTIDINE RESIDUES; HYDROGEN PEROXIDE REACTION; WILD TYPES;

AMINO ACIDS; BINDING SITES; CASE HARDENING; CYANIDES; DISSOCIATION; HYDROGEN; HYDROGEN PEROXIDE; PLANTS (BOTANY); PORPHYRINS; RATE CONSTANTS;

HEMOGLOBIN;

CYANIDE; CYTOCHROME C PEROXIDASE; ENZYME; H52L ENZYME; H52W ENZYME; HEMOPROTEIN; HISTIDINE; HYDROGEN PEROXIDE; UNCLASSIFIED DRUG; W51H ENZYME;

ABSORPTION SPECTROSCOPY; ARTICLE; CLONING; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PURIFICATION; SACCHAROMYCES CEREVISIAE; WILD TYPE;

CYANIDES; CYTOCHROME-C PEROXIDASE; ELECTRON SPIN RESONANCE SPECTROSCOPY; HISTIDINE; HYDROGEN PEROXIDE; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; MUTATION; PROTEIN CONFORMATION;

EID: 67049117938     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9003974     Document Type: Article

References (38)

1. Zamocky, M., Regelsberger, Jakopitsch, C., and Obinger, C. (2001) The molecular peculiarities of catalase-peroxidase. FEBS Lett. 492, 177-182.
2. Takano, T. (1977) Structure of myoglobin refined at 2.0 Å resolution. I. Crystallographic refinement of metmyoglobin from sperm whale. J. Mol. Biol. 110, 537-568.
3. Finzel, B. C., Poulos, T. L., and Kraut, J. (1984) Crystal structure of yeast cytochrome c peroxidase refined at 1.7-Å resolution. J. Biol. Chem. 259, 13027-13036.
4. Dolphin, D., Forman, A., Borg, D. C., Fajer, J., and Felton, R. H. (1971) Compounds I of catalase and horseradish peroxidase: π-cation radicals. Proc. Natl. Acad. Sci. U.S.A. 68, 614-618.
5. Erman, J. E., Vitello, L. B., Mauro, J. M., and Kraut, J. (1989) Detection of an oxyferryl porphyrin π-cation-radical intermediate in the reaction between hydrogen peroxide and a mutant yeast cytochrome c peroxidase: Evidence for tryptophan-191 involvement in the radical site of compound I. Biochemistry 28, 7992-7995. (Pubitemid 19252878)
6. King, N. K., Looney, F. D., and Winfield, M. E. (1964) Myoglobin free radicals. Biochim. Biophys. Acta 88, 235-236.
7. Erman, J. E., Vitello, L. B., Miller, M. A., and Kraut, J. (1992) Activesite mutations in cytochrome c peroxidase: A critical role for histidine-52 in the rate of formation of compound I. J. Am. Chem. Soc. 114, 6592-6593.
8. Erman, J. E., Vitello, L. B., Miller, M. A., Shaw, A., Brown, K. A., and Kraut, J. (1993) Histidine 52 is a critical residue for rapid formation of cytochrome c peroxidase compound I. Biochemistry 32, 9798-9806. (Pubitemid 23296827)
9. Newmyer, S. L., and Ortiz de Montellano, P. R. (1995) Horseradish Peroxidase His-42 → Ala, His-42 → Val, and Phe-41 → Ala Mutants. Histidine catalysis and control of substrate access to the heme iron. J. Biol. Chem. 270, 19438-119438
10. Brittain, T., Baker, A. R., Butler, C. S., Little, R. H., Lowe, D. J., Greenwood, C., and Watmough, N. J. (1997) Reaction of variant sperm-whale myoglobins with hydrogen peroxide: The effects of mutating a histidine residue in the haem pocket. Biochem. J. 326, 109-115. (Pubitemid 27386924)
11. Matsui, T., Ozaki, S., Liong, E., Phillips, G. N. Jr., and Watanabe, Y. (1999) Effects of the location of distal histidine in the reaction of myoglobin with hydrogen peroxide. J. Biol. Chem. 274, 2828-2844.
12. Ozaki, S., Roach, M. P., Matsui, T., and Watanabe, T. (2001) Investigations of the role of the distal heme environment and the proximal heme iron ligand in peroxide activation by heme enzymes via molecular engineering of myoglobin. Acc. Chem. Res. 34, 818-825.
13. Savenkova, M. I., Satterlee, J. D., Erman, J. E., Siems, W. F., and Helms, G. L. (2001) Expression, purification, characterization, and NMR studies of highly deuterated recombinant cytochrome c peroxidase. Biochemistry 40, 12123-12131. (Pubitemid 32946553)
14. Takio, K., Titani, K., Ericsson, L. H., and Yonetani, T. (1980) Primary structure of yeast cytochrome c peroxidase II. The complete amino acid sequence. Arch. Biochem. Biophys. 203, 615-6299.
15. Teske, J. G., Savenkova, M. I., Mauro, J. M., Erman, J. E., and Satterlee, J. D. (2000) Yeast cytochrome c peroxidase expression in Escherichia coli and rapid isolation of various highly purified holoenzymes. Protein Expression Purif. 19, 139-147. (Pubitemid 30387905)
16. Fishel, L. A., Villafranca, J. E., Mauro, J. M., and Kraut, J. (1987) Yeast cytochrome c peroxidase: Mutagenesis and expression in Escherichia coli show tryptophan-51 is not the radical site in compound I. Biochemistry 26, 351-360. (Pubitemid 17022104)
17. 15N-labeled eukaryotic cytochrome c in Escherichia coli. J. Biol. Inorg. Chem. 4, 220-222.
18. Pollock, W. B. R., Rosell, F. I., Twitchett, M. B., Dumont, M. E., and Mauk, A. G. (1998) Bacterial expression of a mitochondrial cytochrome c. Trimethylation of Lys72 in yeast iso-1-cytochrome c and the alkaline conformational transition. Biochemistry 37, 6124-6131.
19. Kolthoff, I. M., and Belcher, R. (1957) Hydrogen peroxide. In Volumetric Analysis, Vol.3, pp 75-76, Interscience, New York.
20. 2 solutions in the UV). Anal. Biochem. 49, 474-478.
21. Berry, E. A., and Trumpower, B. L. (1987) Simultaneous determination of hemes a, b, and c from pyridine hemochrome spectra. Anal. Biochem. 161, 1-15.
22. Vitello, L. B., Erman, J. E., Miller, M. A., Mauro, J. M., and Kraut, J. (1992) Effect of Asp-235 → Asn substitution on the absorption spectrum and hydrogen peroxide reactivity of cytochrome c peroxidase. Biochemistry 31, 11524-11535.
23. Antonini, E., and Brunori, M. (1971) in Hemoglobin and myoglobin in their reactions with ligands, North-Holland Publishing Co., Amsterdam.
24. Erman, J. E., and Yonetani, T. (1975) A kinetic study of the endogenous reduction of the oxidized sites in the primary cytochrome c peroxidase-hydrogen peroxide compound. Biochim. Biophys. Acta 393, 350-357.
25. Erman, J. E. (1974) Kinetic and equilibriumstudies of cyanide binding by cytochrome c peroxidase. Biochemistry 13, 39-44.
26. Smith, D. W., and Williams, R. J. P. (1968) Analysis of the visible spectra of some sperm-whale ferrimyoglobin derivatives. Biochem. J. 110, 297-301.
27. Iizuka, T., and Yonetani, T. (1970) Spin changes in hemoproteins. Adv. Biophys. 1, 157-182.
28. Savenkova, M. I., Newmyer, S. L., and Ortiz de Montellano, P. R. (1996) Rescue of His-42 → Ala horseradish peroxidase by a Phe-41 → His mutation: Engineering of a surrogate catalytic histidine. J. Biol. Chem. 271, 24598-24603.
29. Brancaccio, A., Cutruzzolá, F., Allocatelli, C. T., Brunori, M., Smerdon, S. J., Wilkinson, A. J., Dou, Y., Keenan, D., Ikeda-Sato, M., Brantley, R. E. Jr., and Olson, J. S. (1994) Structural factors governing azide and cyanide binding to mammalian metmyoglobins. J. Biol. Chem. 269, 13842-13853.
30. Savenkova, M. I., Kuo, J. M., and Ortiz de Montellano, P. R. (1998) Improvement of peroxygenase activity by relocation of a catalytic histidine with the active site of horseradish peroxidase. Biochemistry 37, 10828-10836.
31. Alayash, A. I., Ryan, B. A. B., Eich, R. F., Olson, J. S., and Cashon, R. E. (1999) Reactions of sperm whale myoglobin with hydrogen peroxide: Effects of distal pocket mutations on the formation and stability of the ferryl intermediate. J. Biol. Chem. 274, 2029-2037.
32. Wan, L., Twitchett, M. B., Eltis, L. D., Mauk, A. G., and Smith, M. (1998) In vitro evolution of horse heart myoglobin to increase peroxidase activity. Proc. Natl. Acad. Sci. U.S.A. 95, 12825-12831.
33. Matsui, T., Ozaki, S., and Watanabe, Y. (1999) Formation and catalytic roles of compound I in the hydrogen peroxide-dependent oxidations by His64 myoglobin mutants. J. Am. Chem. Soc. 121, 9952-9957.
34. Coulson, A. F. W., Erman, J. E., and Yonetani, T. (1971) Studies on cytochrome c peroxidase. XVII. Stoichiometry and mechanism of the reaction of compound ES with donors. J. Biol. Chem. 246, 917-924.
35. Pearl, N. M., Jacobson, T., Arisa, M., Vitello, L. B., and Erman, J. E. (2007) Effect of single-site charge-reversal mutations on the catalytic properties of yeast cytochrome c peroxidase: Mutations near the high-affinity cytochrome c binding site. Biochemistry 46, 8263-8272. (Pubitemid 47075966)
36. Dou, Y., Olson, J. S., Wilkinson, A. J., and Ikeda-Saito, M. (1996) Mechanism of hydrogen cyanide binding to myoglobin. Biochemistry 35, 7107-7113. (Pubitemid 26182101)
37. Erman, J. E., and Vitello, L. B. (2002) Yeast cytochrome c peroxidase: Mechanistic stdies via protein engineering. Biochim. Biophys. Acta 1597, 193-220.
38. Fita, I., and Rossman, M. G. (1985) The active center of catalase. J. Mol. Biol. 185, 21-37.