Effects of metal ions in the CuB center on the redox properties of heme in heme-copper oxidases: Spectroelectrochemical studies of an engineered heme-copper center in myoglobin

Biochemistry

Volumn 44, Issue 4, 2005, Pages 1210-1214

  Zhao, Xuan ^a   Yeung, Natasha ^a   Wang, Zhilin ^b   Guo, Zijian ^b   Lu, Yi ^a  

^a UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

^b NANJING UNIVERSITY   (China)

Author keywords

[No Author keywords available]

Indexed keywords

COPPER; ELECTROCHEMISTRY; IRON; NEGATIVE IONS; REDOX REACTIONS; REDUCTION; THERMODYNAMICS; ZINC;

BRIDGING LIGANDS; CYANIDE BRIDGE; MYOGLOBIN; UV-VISIBLE SPECTROELECTROCHEMISTRY;

ENZYMES;

COPPER; CYANIDE; HEME; HEME COPPER OXIDASE; HEME OXYGENASE; IRON; MYOGLOBIN; UNCLASSIFIED DRUG;

ARTICLE; ELECTROCHEMICAL ANALYSIS; ENZYME ANALYSIS; LIGAND BINDING; METAL BINDING; NONHUMAN; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTON TRANSPORT; REDUCTION KINETICS; SPECTROSCOPY; THERMODYNAMICS; ULTRAVIOLET SPECTROPHOTOMETRY;

AMINE OXIDASE (COPPER-CONTAINING); ANIMALS; CATIONS, DIVALENT; CATTLE; COPPER; ELECTRON TRANSPORT; ELECTRON TRANSPORT COMPLEX IV; HEME; HISTIDINE; LEUCINE; MYOGLOBIN; OXIDATION-REDUCTION; PHENYLALANINE; POTENTIOMETRY; PROTEIN ENGINEERING; SPECTROPHOTOMETRY, ULTRAVIOLET; WHALES; ZINC;

EID: 13444283384     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0479151     Document Type: Article

References (35)

1. Babcock, G. T., and Wikström, M. (1992) Oxygen activation and the conservation of energy in cell respiration, Nature 356, 301-309.
2. Garcia-Horsman, J. A., Barquera, B., Rumbley, J., Ma, J., and Gennis, R. B. (1994) The superfamily of heme-copper respiratory oxidases, J. Bacteriol. 176, 5587-5600.
3. Ferguson-Miller, S., and Babcock, G. T. (1996) Heme/Copper Terminal Oxidases, Chem. Rev. 96, 2889-2907.
4. Namslauer, A., and Brzezinski, P. (2004) Structural elements involved in electron-coupled proton transfer in cytochrome c oxidase, FEBS Lett. 567, 103-110.
5. Blair, D. F., Ellis, W. R., Jr., Wang, H., Gray, H. B., and Chan, S. I. (1986) Spectroelectrochemical study of cytochrome c oxidase: pH and temperature dependences of the cytochrome potentials. Characterization of site-site interactions, J. Biol. Chem. 261, 11524-11537.
6. Hendler, R. W. and Westerhoff, H. V. (1992) Redox interactions in cytochrome c oxidase: from the "neoclassical" toward "modern" models, Biophys. J. 63, 1586-1604.
7. 3 Contributions and Assignment of Vibrational Modes, Biochemistry 38, 1685-1694.
8. Iwata, S., Ostermeier, C., Ludwig, B., and Michel, H. (1995) Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans, Nature 376, 660-669.
9. Tsukihara, T., Aoyama, H., Yamashita, E., Tomizaki, T., Yamaguchi, H., Shinzawa-Itoh, K., Nakashima, R., Yaono, R., and Yoshikawa, S. (1995) Structures of metal sites of oxidized bovine heart cytochrome c oxidase at 2.8 Å, Science 269, 1069-1074.
10. Yoshikawa, S., Shinzawa-itoh, K., Nakashima, R., Yaono, R., Yamashita, E., Inoue, N., Yao, M., Fei, M. J., Libeu, C. P., Mizushima, T., Yamaguchi, H., Tomizaki, T., and Tsukihara, T. (1998) Redox-coupled crystal structural changes in bovine heart cytochrome c oxidase, Science 280, 1723-1729.
11. Vila, A. J., and Fernandez, C. O. (1996) Structure of the Metal Site in Rhus vernicifera Stellacyanin: A Paramagnetic NMR Study on its Co(II) Derivative, J. Am. Chem. Soc. 118, 7291-7298.
12. Hay, M. T., Milberg, R. M., and Lu, Y. (1996) Preperation and Characterization of Mercury and Silver Derivatives of an Engineered Purple Copper Center in Azurin, J. Am. Chem. Soc. 118, 11976-11977.
13. Lyons, T. J., Nersissian, A., Huang, H., Yeom, H., Nishida, C. R., Graden, J. A., Gralla, E. B., and Valentine, J. S. (2000) The metal binding properties of the zinc site of yeast copper-zinc Superoxide dismutase: implications for amyotrophic lateral sclerosis, J. Biol. Inorg. Chem. 5, 189-203.
14. Hellwig, P., Pfitzner, U., Behr, J., Rost, B., Pesavento, R. P., von Donk, W., Gennis, R. B., Michel, H., Ludwig, B., and Maentele, W. (2002) Vibrational Modes of Tyrosines in Cytochrome c Oxidase from Paracoccus denitrificans: FTIR and Electrochemical Studies on Tyr-D4-labeled and on Tyr280His and Tyr35Phe Mutant Enzymes, Biochemistry 41, 9116-9125.
15. Das, T. K., Pecoraro, C., Tomson, F. L., Gennis, R. B., and Rousseau, D. L. (1998) The Post-translational Modification in Cytochrome c Oxidase Is Required To Establish a Functional Environment of the Catalytic Site, Biochemistry 37, 14471-14476.
16. Lu, Y., Berry, S. M., and Pfister, T. D. (2001) Engineering novel metalloproteins: Design of metal-binding sites into native protein scaffolds, Chem. Rev. 101, 3047-3080.
17. Collman, J. P., Boulatov, R., Sunderland, C. J., and Fu, L. (2004) Functional Analogues of Cytochrome c Oxidase, Myoglobin, and Hemoglobin, Chem. Rev. 104, 561-588.
18. Kim, E., Chufan, E. E., Kamaraj, K., and Karlin, K. D. (2004) Synthetic Models for Heme-Copper Oxidases, Chem. Rev. 104, 1077-1133.
19. Boulatov, R., Collman, J. P., Shiryaeva, I. M., and Sunderland, C. J. (2002) Functional Analogues of the Dioxygen Reduction Site in Cytochrome Oxidase: Mechanistic Aspects and Possible Effects of CuB, J. Am. Chem. Soc. 124, 11923-11935.
20. Varadarajan, R., Zewert, T. E., Gray, H. B., and Boxer, S. G. (1989) Effects of buried ionizable amino acids on the reduction potential of recombinant myoglobin, Science 243, 69-72.
21. B Center into Sperm Whale Myoglobin, J. Am. Chem. Soc. 122, 8192-8196.
22. Sigman, J. A., Kim, H. K., Zhao, X., Carey, J. R., and Lu, Y. (2003) The role of copper and protons in heme-copper oxidases: Kinetic study of an engineered heme-copper center in myoglobin, Proc. Natl. Acad. Sci., U.S.A. 100, 3629-3634.
23. Taboy, C. H., Bonaventura, C., and Crumbliss, A. L. (2002) Anaerobic oxidations of myoglobin and hemoglobin by spectroelectrochemistry, Methods Enzymol. 353, 187-209.
24. Brunori, M., Saggese, U., Rotilio, G. C., Antonini, E., and Wyman, J. (1971) Redox equilibrium of sperm-whale myoglobin, Aplysia myoglobin, and Chironomus thummi hemoglobin, Biochemistry 10, 1604-1609.
25. Lloyd, E., King, B. C., Hawkridge, F. M., and Mauk, A. G. (1998) Electrostatic Modulation of Ligand Binding and Electrochemical Properties of Myoglobin: The Role of Charge Compensation, Inorg. Chem. 37, 2888-2892.
26. King, B. C., Hawkridge, F. M., and Hoffman, B. M. (1992) Electrochemical studies of cyanometmyoglobin and metmyoglobin: implications for long-range electron transfer in proteins, J. Am. Chem. Soc. 114, 10603-10608.
27. Kannt, A., Lancaster, C. R. D., and Michel, H. (1998) The role of electrostatic interactions for cytochrome c oxidase function, J. Bioenerg. Biomembr. 30, 81-87.
28. Michel, H. (1999) Cytochrome c Oxidase: Catalytic Cycle and Mechanisms of Proton Pumping-A Discussion, Biochemistry 38, 15129-15140.
29. Verkhovsky, M. I., Morgan, J. E., and Wikstroem, M. (1995) Control of electron delivery to the oxygen reduction site of cytochrome c oxidase: A role for protons, Biochemistry 34, 7483-7491.
30. Aedelroth, P., Sigurdson, H., Hallen, S., and Brzeanski, P. (1996) Kinetic coupling between electron and proton transfer in cytochrome c oxidase: simultaneous measurements of conductance and absorbance changes, Proc. Natl. Acad. Sci. U.S.A. 93, 12292-12297.
31. Aedelroth, P., Brzezinski, P., and Malmstroem, B. G. (1995) Internal Electron Transfer in Cytochrome c Oxidase from Rhodobacter sphaeroides, Biochemistry 34, 2844-2849.
32. Juenemann, S., Meunier, B., Gennis, R. B., and Rich, P. R. (1997) Effects of Mutation of the Conserved Lysine-362 in Cytochrome c Oxidase from Rhodobacter sphaeroides, Biochemistry 36, 14456-14464.
33. Karpefors, M., Adelroth, P., Aagaard, A., Sigurdson, H., Ek, M. S., and Brzezinski, P. (1998) Electron-proton interactions in terminal oxidases, Biochim. Biophys. Acta 1365, 159-169.
34. 3-Type Quinol Oxidase from Bacillus subtilis: An ENDOR and EXAFS Study, Biochemistry 34, 10245-10255.
35. Braenden, M., Namslauer, A., Hansson, O., Aasa, R., and Brzezinski, P. (2003) Water-Hydroxide Exchange Reactions at the Catalytic Site of Heme-Copper Oxidases, Biochemistry 42, 13178-13184.