The use of stable isotopes and spectroscopy to investigate the energy transducing function of cytochrome c oxidase

Biochimica et Biophysica Acta - Bioenergetics

Volumn 1655, Issue 1-3, 2004, Pages 248-255

  Schmidt, Bryan ^a,b   Hillier, Warwick ^b   McCracken, John ^b   Ferguson Miller, Shelagh ^a  

^a Michigan State University   (United States)

^b MICHIGAN STATE UNIVERSITY   (United States)

Author keywords

Cytochrome aa3; EPR; FTIR; Heme; Stable isotope; Water

Indexed keywords

CYTOCHROME C OXIDASE; HEME; HISTIDINE; MAGNESIUM; MANGANESE; NITROGEN 15; OXYGEN 17; STABLE ISOTOPE;

ANALYTIC METHOD; ELECTROCHEMICAL ANALYSIS; ELECTRON SPIN RESONANCE; ENERGY TRANSFER; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME MECHANISM; FOURIER ANALYSIS; NONHUMAN; PRIORITY JOURNAL; REVIEW; SPECIES DIFFERENCE;

ANIMALS; CATTLE; ELECTROCHEMISTRY; ELECTRON SPIN RESONANCE SPECTROSCOPY; ELECTRON TRANSPORT COMPLEX IV; ENERGY METABOLISM; HEME; HISTIDINE; MANGANESE; MODELS, BIOLOGICAL; NITROGEN ISOTOPES; OXYGEN ISOTOPES; RHODOBACTER SPHAEROIDES; SPECTROSCOPY, FOURIER TRANSFORM INFRARED;

BACTERIA (MICROORGANISMS); BOVINAE;

EID: 1942536502     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2003.11.008     Document Type: Review

References (43)

1. C?)ZnMg. Chem. Scr. 28A:1988;35-40.
2. Ferguson-Miller S., Babcock G.T. Heme/copper terminal oxidases. Chem. Rev. 96:1996;2889-2907.
3. Tsukihara T., Aoyama H., Yamashita E., Tomizaki T., Yamaguchi H., Shinzawaitoh K., Nakashima R., Yaono R., Yoshikawa S. Structures of metal sites of oxidized bovine heart cytochrome c oxidase at 2.8 Å Science. 269:1995;1069-1074.
4. Iwata S., Ostermeier C., Ludwig B., Michel H. Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature. 376:1995;660-669.
5. Aasa R., Albracht P.J., Falk K.-E., Lanne B., Vänngård T. EPR signals from cytochrome c oxidase. Biochim. Biophys. Acta. 422:1976;260-272.
6. Beinert H., Hansen R.E., Hartzell C.R. Kinetic studies of cytochrome c oxidase by combined EPR and reflectance spectroscopy after rapid freezing. Biochim. Biophys. Acta. 423:1976;339-355.
7. Clore G.M., Andréasson L.E., Karlsson B., Aasa R., Malmstrom B.G. Characterization of the low-temperature intermediates of the reaction of fully reduced soluble cytochrome oxidase with oxygen by electron paramagnetic resonance and optical spectroscopy. Biochem. J. 185:1980;139-154.
8. Callahan P.M., Babcock G.T. Origin of the cytochrome a absorption red shift: a pH dependent interaction between its heme a formyl and protein in cytochrome oxidase. Biochemistry. 22:1983;452-461.
9. Antonini G., Malatesta F., Sarti P., Brunori M. Proton pumping by cytochrome oxidase as studied by time-resolved stopped-flow spectrophotometry. Proc. Natl. Acad. Sci. U. S. A. 90:1993;5949-5953.
10. Szundi I., Cappuccio J.A., Borovok N., Kotlyar A.B., Einarsdóttir Ó. Photoinduced electron transfer in the cytochrome c/cytochrome c oxidase complex using thiouredopyrenetrisulfonate-labeled cytochrome c optical multichannel detection. Biochemistry. 40:2001;2186-2193.
11. Liebl U., Lipowski G., Negrerie M., Lambry J.C., Martin J.L., Vos M.H. Coherent reaction dynamics in a bacterial cytochrome c oxidase. Nature. 401:1999;181-184.
12. Mills D.A., Schmidt B., Hiser C., Westley E., Ferguson-Miller S. Membrane potential-controlled inhibition of cytochrome c oxidase by zinc. J. Biol. Chem. 277:2002;14894-14901.
13. Mills D.A., Florens L., Hiser C., Qian J., Ferguson-Miller S. Where is 'outside' in cytochrome c oxidase and how and when do protons get there? Biochim. Biophys. Acta. 1458:2000;180-187.
14. Mills D.A., Ferguson-Miller S. Proton uptake and release in cytochrome c oxidase: separate pathways in time and space? Biochim. Biophys. Acta. 1365:1998;46-52.
15. Hellwig P., Rost B., Mäntele W. Redox dependent conformational changes in the mixed valence form of the cytochrome c oxidase from P. denitrificans: the reorganization of glutamic acid 278 is coupled to the electron transfer from/to heme a and the binuclear center. Spectrochim. Acta, Part A: Mol. Biomol. Spectrosc. 57:2001;1123-1131.
16. Hosler J.P., Espe M.P., Zhen Y.J., Babcock G.T., Ferguson-Miller S. Analysis of site-directed mutants locates a non-redox-active metal near the active site of cytochrome c oxidase of Rhodobacter sphaeroides. Biochemistry. 34:1995;7586-7592.
17. Florens L., Schmidt B., McCracken J., Ferguson-Miller S. Fast deuterium access to the buried magnesium/manganese site in cytochrome c oxidase. Biochemistry. 40:2001;7491-7497.
18. Schmidt B., McCracken J., Ferguson-Miller S. A discrete water exit pathway in the membrane protein cytochrome c oxidase. Proc. Natl. Acad. Sci. U. S. A. 100:2003;15539-15542.
19. Morgan J.E., Verkhovsky M.I., Wikström M. The histidine cycle: a new model for proton translocation in the respiratory heme-copper oxidases. J. Bioenerg. Biomembranes. 26:1994;599-608.
20. Wikström M., Bogachev A., Finel M., Morgan J.E., Puustinen A., Raitio M., Verkhovskaya M., Verkhovsky M.I. Mechanism of proton translocation by the respiratory oxidases: the histidine cycle. Biochim. Biophys. Acta. 1187:1994;106-111.
21. Michel H. Cytochrome c oxidase: catalytic cycle and mechanisms of proton pumping - a discussion. Biochemistry. 38:1999;15129-15140.
22. Capitanio N., Capitanio G., Minuto M., De Nitto E., Palese L.L., Nicholls P., Papa S. Coupling of electron transfer with proton transfer at heme a and CuA (redox Bohr effects) in cytochrome c oxidase. Studies with the carbon monoxide inhibited enzyme. Biochemistry. 39:2000;6373-6379.
23. Marantz Y., Nachliel E., Aagaard A., Brzezinski P., Gutman M. The proton collecting function of the inner surface of cytochrome c oxidase from Rhodobacter sphaeroides. Proc. Natl. Acad. Sci. U. S. A. 95:1998;8590-8595.
24. Hasegawa K., Ono T., Noguchi T. Vibrational spectra and Ab initio DFT calculations of 4-methylimidazole and its different protonation forms: infrared and Raman markers of the protonation state of a histidine side chain. J. Phys. Chem., B. 104:2000;4253-4265.
25. Hasegawa K., Ono T., Noguchi T. Ab initio density functional theory calculations and vibrational analysis of zinc bound 4-methylimidazole as a model of a histidine ligand in metalloenzymes. J. Phys. Chem., A. 106:2002;3377-3390.
26. Svensson-Ek M., Abramson J., Larsson G., Tornroth S., Brzezinski P., Iwata S. The X-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides. J. Mol. Biol. 321:2002;329-339.
27. Callahan P.M., Babcock G.T. Insights into heme structure from Soret excitation Raman spectroscopy. Biochemistry. 20:1981;952-958.
28. Babcock G.T. Spiro T.G. Biological Applications of Raman Spectroscopy. 1988;293-346 Wiley, New York.
29. B center. Proc. Natl. Acad. Sci. U. S. A. 89:1992;4786-4790.
30. Proshlyakov D.A., Pressler M.A., Babcock G.T. Dioxygen activation and bond cleavage by mixed-valence cytochrome c oxidase. Proc. Natl. Acad. Sci. U. S. A. 95:1998;8020-8025.
31. Behr J., Hellwig P., Mäntele W., Michel H. Redox dependent changes at the heme propionates in cytochrome c oxidase from Paracoccus denitrificans: direct evidence from FTIR difference spectroscopy in combination with heme propionate 13C labeling. Biochemistry. 37:1998;7400-7406.
32. Behr J., Michel H., Mäntele W., Hellwig P. Functional properties of the heme propionates in cytochrome c oxidase from Paracoccus denitrificans. Evidence from FTIR difference spectroscopy and site-directed mutagenesis. Biochemistry. 39:2000;1356-1363.
33. Barth A. The infrared absorption of amino acid side chains. Prog. Biophys. Mol. Biol. 74:2000;141-173.
34. Choi S., Lee J.J., Wei Y.H., Spiro T.G. Resonance Raman and electronic spectra of heme a complexes and cytochrome oxidase. J. Am. Chem. Soc. 105:1983;3692-3707.
35. Hu S.Z., Smith K.M., Spiro T.G. Assignment of protoheme resonance Raman spectrum by heme labeling in myoglobin. J. Am. Chem. Soc. 118:1996;12638-12646.
36. 3. Biochemistry. 41:2002;967-973.
37. 3 contributions and assignment of vibrational modes. Biochemistry. 38:1999;1685-1694.
38. Ludwig B., Bender E., Arnold S., Huttemann M., Lee I., Kadenbach B. Cytochrome c oxidase and the regulation of oxidative phosphorylation. ChemBioChem. 2:2001;392-403.
39. Hellwig P., Behr J., Ostermeier C., Richter O.M.H., Pfitzner U., Odenwald A., Ludwig B., Michel H., Mäntele W. Involvement of glutamic acid 278 in the redox reaction of the cytochrome c oxidase from Paracoccus denitrificans investigated by FTIR spectroscopy. Biochemistry. 37:1998;7390-7399.
40. 3. Biochemistry. 38:1999;2048-2056.
41. B in cytochrome c oxidase is dynamically linked to structural changes around a carboxyl group: a time-resolved step-scan Fourier transform infrared investigation. Biophys. J. 82:2002;1-10.
42. Helwig P., Soulimane T., Buse G., Mantele W. Similarities and dissimilarities in the structure-function relation between the cytochrome c oxidase from bovine heart and from Paracoccus denitrificans as revealed by FT-IR difference spectroscopy. FEBS Lett. 458:1999;83-86.
43. 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., Tsukihara T. Redox-coupled crystal structural changes in bovine heart cytochrome c oxidase. Science. 280:1998;1723-1729.