Relationships between Structure and Function in Cytochrome Oxidase (original) (raw)

References

• Alben, J. O., Moh, P. P., Fiamingo, F. G., and Altschuld, R. A., 1981, Cytochrome oxidase (a 3) heme and copper observed by low-temperature Fourier transform infrared spectroscopy of the CO complex, Proc. Natl. Acad. Sci. USA 78:234–237.
  Article PubMed CAS Google Scholar
• Anderson, S., Bankier, A. T., Barrell, B. G., de Bruijn, M. H. L., Coulson, A. R., Drouin, J., Eperon, I. C., Nierlich, D. P., Roe, B. A., Sanger, F., Schreier, P. H., Smith, A. J. H., Staden, R., and Young, I. G., 1981, Sequence and organization of the human mitochondrial genome, Nature 290:457–465.
  Article PubMed CAS Google Scholar
• Anderson, S., de Bruijn, M. H. L., Coulson, A. R., Eperon, I. C., Sanger, F., and Young, I. G., 1982, Complete sequence of bovine mitochondrial DNA. Conserved features of the mammalian mitochondrial genome, J. Mol. Biol. 156:683–717.
  Article PubMed CAS Google Scholar
• Antalis, T. M., and Palmer, G., 1982, Kinetic characterization of the interaction between cytochrome oxidase and cytochrome c. J. Biol. Chem. 257:6194–6206.
  PubMed CAS Google Scholar
• Artzatbanoy, V. Yu., Konstantinov, A. A., and Skulachev, V. P., 1978, Involvement of intramitochondrial protons in redox reactions of cytochrome a, FEBS Lett. 87:180–185.
  Article Google Scholar
• Azzi, A., 1980, Cytochrome c oxidase. Towards a clarification of its structure, interactions and mechanism, Biochim. Biophys. Acta 594:231–252.
  Article PubMed CAS Google Scholar
• Azzi, A., Bill, K., Bolli, R., Broger, C., Casey, R. P., and Corbley, M., 1982, On the Structure of Cytochrome c Oxidase and the Location of its Active Centers. 2nd Eur. Bioenerg. Conf. Short Reports, L.B.T.M.-C.N.R.S. éditeur, Villeurbanne, pp. 125–126.
  Google Scholar
• Babcock, G. T., and Salmeen, I., 1979, Resonance Raman spectra and optical properties of oxidized cytochrome oxidase, Biochemistry 18:2493–2498.
  Article PubMed CAS Google Scholar
• Babcock, G. T., Vickery, L. E., and Palmer, G., 1976, Electronic state of heme in cytochrome oxidase. I. Magnetic circular dichroism of the isolated enzyme and its derivatives, J. Biol. Chem. 251:7907–7919.
  PubMed CAS Google Scholar
• Babcock, G. T., Van Steelandt, J., Palmer, G., Vickery, L. E., and Salmeen, I., 1979, Heme a models for cytochromes a and a 3 in cytochrome oxidase—EPR, MCD and resonance Raman studies, in: Cytochrome Oxidase (T. E. King, Y. Orii, B. Chance, and K. Okunuki, eds.) Amsterdam, New York, and Oxford, Elsevier/North-Holland pp. 105–115.
  Google Scholar
• Babcock, G. T., Callahan, P. M., Ondrias, M. R., and Salmeen, I., 1981, Coordination geometries and vibrational properties of the cytochromes a and a 3 in cytochrome oxidase from soret excitation Raman spectroscopy, Biochemistry 20:959–966.
  Article PubMed CAS Google Scholar
• Bibb, M. J., Van Etten, R. A., Wright, C. T., Walberg, M. W., and Clayton, D. A., 1981, Sequence and gene organization of mouse mitochondrial DNA, Cell 26:167–180.
  Article PubMed CAS Google Scholar
• Birchmeyer, W., Köhler, C. E., and Schatz, G., 1976, Interaction of integral and peripheral membrane proteins: Affinity labelling of yeast cytochrome oxidase by modified yeast cytochrome c, Proc. Natl. Acad. Sci. USA 73:4334–4338.
  Article Google Scholar
• Bisson, R., and Montecucco, C., 1982, Different polypeptides of bovine heart cytochrome c oxidase are in contact with cytochrome c, FEBS Lett. 150:49–53.
  Article PubMed CAS Google Scholar
• Bisson, R., Montecucco, C., Gutweniger, H., and Azzi, A., 1978, Photoaffinity labels for the study of cytochrome c and phospholipid interactions with cytochrome c oxidase, in: Frontiers of Biological Energetics, Vol. 2 (P. L. Dutton, J. S. Leigh, Jr., and A. Scarpa, eds.), Academic Press, New York, pp. 809–816.
  Google Scholar
• Bisson, R., Steffens, G. C. M., and Buse, G., 1982a, Localization of lipid binding domains on subunit II of beef heart cytochrome c oxidase, J. Biol. Chem. 257:6716–6720.
  PubMed CAS Google Scholar
• Bisson, R., Steffens, G. C. M., Capaldi, R. A., and Buse, G., 1982b, Mapping of the cytochrome c binding site on cytochrome c oxidase, FEBS Lett. 144:359–363.
  Article PubMed CAS Google Scholar
• Blasie, J. K., Erecinska, M., Samuels, S., and Leigh, J. S., 1978, The structure of a cytochrome oxidaselipid model membrane, Biochim. Biophys. Acta 501:33–52.
  Article PubMed CAS Google Scholar
• Blasie, J. K., Pachence, J. M., Tavormina, A., Dutton, P. L., Stamatoff, J., Eisenberger, P., and Brown, G., 1982, The location of redox centres in biological membranes determined by resonance X-ray diffraction. II. Analysis of the resonance diffraction data, Biochim. Biophys. Acta 679:188–197.
  Article PubMed CAS Google Scholar
• Blokzijl-Homan, M. F. J., and Van Gelder, B. F., 1971, Biochemical and biophysical studies on cytochrome aa 3. III. The EPR spectrum of NO-ferrocytochrome a 3, Biochim. Biophys. Acta 234:493–498.
  Article PubMed CAS Google Scholar
• Blum, H., Harmon, H. J., Leigh, J. S., Salerno, J. C., and Chance, B., 1978, The orientation of a heme of cytochrome c oxidase in submitochondrial particles, Biochim. Biophys. Acta 502:1–10.
  Article PubMed CAS Google Scholar
• Blumberg, W. E., and Peisach, J., 1979, Some possible chemical and electronic states of cytochrome c oxidase and its intermediate redox states, in: Cytochrome Oxidase (T. E. King, Y. Orii, B. Chase, and K. Okunuki, eds.), Elsevier/North-Holland Biomedical Press, Amsterdam, New York, and Oxford, pp. 153–159.
  Google Scholar
• Bonitz, S. G., Coruzzi, C., Thalenfeld, B. E., Tzagoloff, A., and Macino, G., 1980, Assembly of mitochondrial membrane system. Structure and nucleotide sequence of the gene coding for subunit I of yeast cytochrome oxidase, J. Biol. Chem. 255:11927–11941.
  PubMed CAS Google Scholar
• Boogaart, P., van den, van Dijk, S., and Agsteribbe, E., 1982, The mitochondrially made subunit 2 of Neurospora crassa cytochrome aa 3 is synthesized as a precursor protein, FEBS Lett. 147:97–100.
  Article PubMed Google Scholar
• Brown, G. G., and Simpson, M. V., 1982, Novel features of animal mtDNA evolution as shown by sequences of two rat cytochrome oxidase subunit II genes, Proc. Natl. Acad. Sci. USA 79:3246–3250.
  Article PubMed CAS Google Scholar
• Browning, K. S., and Raj Bhandary, U. L., 1982, Cytochrome oxidase subunit III gene in Neurospora crassa mitochondria. Location and sequence, J. Biol. Chem. 257:5253–5256.
  PubMed CAS Google Scholar
• Brudvig, G. W., Stevens, T. H., and Chan, S. I., 1980, Reactions of nitric oxide with cytochrome c oxidase, Biochemistry 19:5275–5285.
  Article PubMed CAS Google Scholar
• Burger, G., Scriven, C., Machleidt, W., and Werner, S., 1982, Subunit I of cytochrome oxidase from Neurospora crassa: Nucleotide sequence of the coding gene and partial amino acid sequence of the protein, EMBO J. 1:1385–1391.
  PubMed CAS Google Scholar
• Buse, G., Steffens, G. C. M., Steffens, G. J., Meinecke, L., Biewald, R., and Erdweg, M., 1982, Cytochrome c Oxidase: Present Status of the Sequence Analysis, 2nd Eur. Bioenerg. Conf. Short Reports, L.B.T.M.-C.N.R.S. éditeur, Villeurbanne, France, pp. 163–164.
  Google Scholar
• Callahan, P. M., and Babcock, G. T., 1984, The origin of the cytochrome a absorption red shift: A pH dependent interaction between its heme a formyl and protein in cytochrome oxidase, Biochemistry, in press.
  Google Scholar
• Capaldi, R. A., 1982, Arrangement of proteins in the mitochondrial inner membrane, Biochim. Biophys. Acta 694:291–306.
  Article PubMed CAS Google Scholar
• Capaldi, R. A., Darley-Usmar, V., Fuller, S. D., and Georgevich, G., 1981, Structure and functioning of cytochrome c oxidase, in: Vectorial Reactions in Electron and Ion Transport in Mitochondria and Bacteria (F. Palmieri, E. Quagliariello, N. Siliprandi, and E. C. Slater, eds.), Elsevier/North-Holland Biomedical Press, Amsterdam, pp. 25–35.
  Google Scholar
• Capaldi, R. A., Darley-Usmar, V., Fuller, S., and Millett, F., 1982, Structural and functional features of the interaction of cytochrome c with complex III and cytochrome c oxidase, FEBS Lett. 138:1–7.
  Article PubMed CAS Google Scholar
• Carithers, R. P., and Palmer, G., 1981, Characterization of the potentiometric behavior of soluble cytochrome oxidase by magnetic circular dichroism, J. Biol. Chem. 256:7967–7976.
  PubMed CAS Google Scholar
• Casey, R. P., Thelen, M., and Azzi, A., 1980, Dicyclohexylcarbodiimide binds specifically and covalently to cytochrome c oxidase while inhibiting its H+-translocating activity, J. Biol. Chem. 255:3994–4000.
  PubMed CAS Google Scholar
• Caughey, W. S., Smythe, G. A., O’Keeffe, D. H., Maskasky, J. E., and Smith, M. L., 1975, Heme A of cytochrome c oxidase. Structure and properties: Comparisons with hemes B, C, and S and derivatives, J. Biol. Chem. 250:7602–7622.
  PubMed CAS Google Scholar
• Chan, S. I., Brocian, D. F., Brudvig, G. W., Morse, R. H., and Stevens, T. H., 1978, A model for the “visible” copper in cytochrome c oxidase, in: Frontiers of Biological Energetics, Vol. 2 (P. L. Dutton, J. S. Leigh, Jr., and A. Scarpa, eds.), Academic Press, New York, pp. 883–888.
  Google Scholar
• Chan, S. I., Bocian, D. F., Brudvig, G. W., Morse, R. H., and Stevens, T. H., 1979, The nature of the “visible” copper in cytochrome c oxidase, in: Cytochrome Oxidase (T, E. King, Y. Orii, B. Chase, and K. Okunuki, eds.), Elsevier/North-Holland Biomedical Press, Amsterdam, pp. 177–188.
  Google Scholar
• Chance, B., Saronio, C., and Leigh, J. S., Jr., 1975, Functional intermediates in the reaction of membrane-bound cytochrome oxidase with oxygen, J. Biol. Chem. 250:9226–9237.
  PubMed CAS Google Scholar
• Chothia, C., and Lesk, A. M., 1982, Evolution of proteins formed by β-sheets. I. Plastocyanin and azurin, J. Mol. Biol. 160:309–323.
  Article PubMed CAS Google Scholar
• Clore, G. M., Andréasson, L.-E., Karlsson, B., Aasa, R., and Malmström, B. G., 1980, Characterization of the low-temperature intermediates of the reaction of fully reduced soluble cytochrome c oxidase with oxygen by electron paramagnetic resonance and optical spectroscopy, Biochem. J. 185:139–154.
  PubMed CAS Google Scholar
• Coruzzi, G., and Tzagoloff, A., 1979, Assembly of mitochondrial membrane systems. DNA sequence of subunit 2 of yeast cytochrome oxidase, J. Biol. Chem. 254:9324–9330.
  PubMed CAS Google Scholar
• Darley-Usmar, V., Capaldi, R. A., and Wilson, M. T., 1981, Identification of cysteines in subunit II as ligands to the redox centers of bovine cytochrome c oxidase, Biochem. Biophys. Res. Commun. 103:1223–1230.
  Article PubMed CAS Google Scholar
• Deatherage, J. F., Henderson, R., and Capaldi, R. A., 1982a, Three-dimensional structure of cytochrome c oxidase vesicle crystals in negative stain, J. Mol. Biol. 158:487–499.
  Article PubMed CAS Google Scholar
• Deatherage, J. F., Henderson, R., and Capaldi, R. A., 1982b, Relationship between membrane and cytoplasmic domains in cytochrome c oxidase by electron microscopy in media of different density, J. Mol. Biol. 158:501–514.
  Article PubMed CAS Google Scholar
• Dockter, M. E., Steinemann, A., and Schatz, G., 1978, Mapping of yeast cytochrome c oxidase by fluorescence resonance energy transfer, J. Biol. Chem. 253:311–317.
  PubMed CAS Google Scholar
• Edmundson, A. B., 1965, Amino acid sequence of sperm whale myoglobin, Nature 205:883–887.
  Article CAS Google Scholar
• Eklund, H., Nordstrom, B., Zeppezauer, E., Söderlund, G., Ohlsson, I., Boiwe, T., Söderberg, B., Tapia, O., Brändén, C., and Åkeson, Å., 1976, Three-dimensional structure of horse liver alcohol dehydrogenase at 2.4 Å resolution, J. Mol. Biol. 102:27–59.
  Article PubMed CAS Google Scholar
• Erecinska, M., 1977, A new photoaffinity-labeled derivative of mitochondrial cytochrome c, Biochem. Biophys. Res. Commun. 76:495–501.
  Article CAS Google Scholar
• Erecinska, M., and Wilson, D. F., 1978, Cytochrome c oxidase: A synopsis, Arch. Biochem. Biophys. 188:1–14.
  Article PubMed CAS Google Scholar
• Erecinska, M., Blasie, J. K., and Wilson, D. F., 1977, Orientation of the hemes of cytochrome c oxidase and cytochrome c in mitochondria, FEBS Lett. 76:235–239.
  Article PubMed CAS Google Scholar
• Erecińska, M., Wilson, D. F., and Blasie, J. K., 1979, Studies of the orientation of the mitochondrial redox carriers. III. Orientation of the g x and g y axes of the hemes of cytochrome oxidase with respect to the plane of the membrane in oriented membrane multilayers, Biochim. Biophys. Acta 545:352–364.
  Article PubMed Google Scholar
• Falk, K.-E., Vänngård, T., and Ångström, J., 1977, Heme spin-states of cytochrome c oxidase derived from room temperature magnetic susceptibility measurements, FEBS Lett. 75:23–27.
  Article PubMed CAS Google Scholar
• Ferguson-Miller, S., Brautigan, D. L., and Margoliash, E., 1978, Definition of cytochrome c binding domains by chemical modification. III. Kinetics of reaction of carboxydinitrophenyl cytochromes c with cytochrome c oxidase, J. Biol. Chem. 253:149–159.
  PubMed CAS Google Scholar
• Fiamingo, F. G., Altschuld, R. A., Moh, P. P., and Alben, J. O., 1982, Dynamic interactions of CO with a3Fe and CuB in cytochrome c oxidase in beef heart mitochondria studied by Fourier transform infrared spectroscopy at low temperatures, J. Biol. Chem. 257:1639–1650.
  PubMed CAS Google Scholar
• Fox, T. D., 1979, Five TGA “stop” codons occur within the translated sequence of the yeast mitochondrial gene for cytochrome c oxidase subunit II, Proc. Natl. Acad. Sci. USA 76:6534–6538.
  Article PubMed CAS Google Scholar
• Fox, T. D., and Leaver, C. J., 1981, The Zea mays mitochondrial gene coding cytochrome oxidase subunit II has an intervening sequence and does not contain TGA codons, Cell 26:315–323.
  Article PubMed CAS Google Scholar
• Freedman, J. A., Tracy, R. P., and Chan, S. P., 1979, Heme-associated subunit complex of cytochrome c oxidase identified by a new two-dimensional gel electrophoresis, J. Biol. Chem. 254:4305–4308.
  PubMed CAS Google Scholar
• Freund, F., 1982, The proton pump at work. Part I. The basic concept of excess proton/defect proton translocation, Bioelectrochem. Bioenerg. 9:61–77.
  Article CAS Google Scholar
• Frey, T. G., Chan, S. H. P., and Schatz, G., 1978, Structure and orientation of cytochrome c oxidase in crystalline membranes, J. Biol. Chem. 253:4389–4395.
  PubMed CAS Google Scholar
• Fuller, S.D., Capaldi, R. A., and Henderson, R., 1979, Structure of cytochrome c oxidase in deoxycholatederived two-dimensional crystals, J. Mol. Biol. 134:305–327.
  Article PubMed CAS Google Scholar
• Fuller, S.D., Darley-Usmar, V.M., and Capaldi, R. A., 1981, Covalent complex between yeast cytochrome c and beef heart cytochrome c oxidase which is active in electron transfer, Biochemistry 20:7046–7053.
  Article PubMed CAS Google Scholar
• Gennis, R. B., Casey, R. P., Azzi, A., and Ludwig, B., 1982, Purification and characterization of the cytochrome c oxidase from Rhodopseudomonas sphaeroides, Eur. J. Biochem. 125:189–195.
  Article PubMed CAS Google Scholar
• Georgevich, G., Darley-Usmar, V. M., Malatesta, F., and Capaldi, R. A., 1984, Electron transfer in monomeric forms of beef and shark heart cytochrome c oxidase, Biochemistry, in press.
  Google Scholar
• Gregor, I., and Tsugita, A., 1982, The amino acid sequence of cytochrome c oxidase subunit IV from Saccharomyces cerevisiae, J. Biol. Chem. 257:13081–13087.
  PubMed CAS Google Scholar
• Hansson, Ö., Karlsson, B., Aasa, R., Vänngård, T., and Malmström, B. G., 1982, EMBO J 1:1295–1297.
  PubMed CAS Google Scholar
• Henderson, R., Capaldi, R. A., and Leigh, J. S., 1977, Arrangement of cytochrome oxidase molecules in two-dimensional vesicle crystals, J. Mol. Biol. 112:631–648.
  Article PubMed CAS Google Scholar
• Hill, T. L., 1977, Biochemical cycles and free energy transduction, TIBS 2:204–207.
  CAS Google Scholar
• Hoffman, B. M., Roberts, J. E., Awanson, M., Speck, S. H., and Margoliash, E., 1980, Copper electronnuclear double resonance of cytochrome c oxidase, Proc. Natl. Acad. Sci. USA 77:1452–1456.
  Article PubMed CAS Google Scholar
• Kadenbach, B., and Merle, P., 1981, On the function of multiple subunits of cytochrome c oxidase from higher eukaroytes, FEBS Lett. 135:1–11.
  Article PubMed CAS Google Scholar
• Kadenbach, B., Hartmann, R., Glanville, R., and Buse, G., 1982, Tissue-specific genes code for polypeptide VIa of bovine liver and heart cytochrome c oxidase, FEBS Lett. 138:236–238.
  Article PubMed CAS Google Scholar
• Kadenbach, B., Jarausch, J., Hartmann, R., and Merle, P., 1984, Separation of mammalian cytochrome c oxidase into 13 polypeptides by an SDS-gel electrophoresis procedure, Anal. Biochem., in press.
  Google Scholar
• King, T. E., Yu, L., Yu, C.-A., and Wei, Y.-H., 1979, Subunits of cytochrome oxidase and their large scale preparations, in: Cytochrome Oxidase (T. E. King, Y. Orii, B. Chase, and K. Okunuki, eds.), Elsevier/North-Holland Biomedical Press, Amsterdam, pp. 53–65.
  Google Scholar
• Koppenol, W. H., and Margoliash, E., 1982, The asymmetric distribution of charges on the surface of horse cytochrome c, J. Biol. Chem. 257:4426–4437.
  PubMed CAS Google Scholar
• Kroneck, P. M. H., Vortisch, V., and Hemmerich, P., 1980, Model studies on the coordination of copper in biological systems, Eur. J. Biochem. 109:603–612.
  Article PubMed CAS Google Scholar
• Kyte, J., and Doolittle, R. F., 1982, A simple method for displaying the hydropathic character of a protein, J. Mol. Biol. 157:105–132.
  Article PubMed CAS Google Scholar
• Lehtovaara, P., and Ellfolk, N., 1975, The amino acid sequence of leghemoglobin component a from Phaseolus vulgaris (kidney bean), Eur. J. Biochem. 54:577–584.
  Article PubMed CAS Google Scholar
• Ludwig, B., 1980, Heme aa 3 type cytochrome c oxidases from bacteria, Biochim. Biophys. Acta 594:177–189.
  Article PubMed CAS Google Scholar
• Ludwig, B., Downer, N. W., and Capaldi, R. A., 1979, Labeling of cytochrome c oxidase with (35S)diazobenzenesulfonate. Orientation of this election transfer complex in the inner mitochondrial membrane, Biochemistry 18:1401–1407.
  Article PubMed CAS Google Scholar
• Ludwig, B., Grabo, M., Gregor, L, Lustig, A., Regenass, M., and Rosenbusch, J. P., 1982, Solubilized cytochrome c oxidase from Paracoccus denitrificans is a monomer, J. Biol. Chem. 257:5576–5578.
  PubMed CAS Google Scholar
• Makinen, M. W., 1979, A comment on the electronic structure of the Fe-O2 group in oxyheme, in: Biochemical and Clinical Aspects of Oxygen (W. S. Caughey, ed.), Academic Press, New York, pp. 143–155.
  Chapter Google Scholar
• Malmström, B. G., 1979, Cytochrome c oxidase. Structure and catalytic activity, Biochim. Biophys. Acta 549:281–303.
  Article PubMed Google Scholar
• Malmström, B. G., 1982, Enzymology of oxygen, Annu. Rev. Biochem. 51:21–59.
  Article PubMed Google Scholar
• Mann, A. J., and Auer, H. E., 1980, Partial inactivation of cytochrome c oxidase by nonpolar mercurial reagents, J. Biol. Chem. 255:454–458.
  PubMed CAS Google Scholar
• Merle, P., and Kadenbach, B., 1980, The subunit composition of mammalian cytochrome c oxidase, Eur. J. Biochem. 105:499–507.
  Article PubMed CAS Google Scholar
• Merle, P., and Kadenbach, B., 1982, Kinetic and structural differences between cytochrome c oxidases from beef liver and heart, Eur. J. Biochem. 125:239–244.
  Article PubMed CAS Google Scholar
• Millett, F., de Jong, C., Paulson, L., and Capaldi, R. A., 1984, Identification of specific carboxylate groups in cytochrome c oxidase that are involved in binding cytochrome c, Biochemistry, in press.
  Google Scholar
• Mims, W. B., Peisach, J., Shaw, R. W., and Beinert, H., 1980, Electron spin echo studies of cytochrome c oxidase, J. Biol. Chem. 255:6843–6846.
  PubMed CAS Google Scholar
• Mitchell, P., 1968, Chemiosmotic Coupling and Energy Transduction, Glynn Research, Bodmin, U.K.
  Google Scholar
• Moss, T. H., Shapiro, E., King, T. E., Beinert, H., and Hartzell, C. R., 1978, The magnetic susceptibility of cytochrome oxidase in the 4.2-1.5K range, J. Biol. Chem. 253:8072–8073.
  PubMed CAS Google Scholar
• Nagle, J. F., and Mille, M., 1981, Molecular models of proton pumps, J. Chem. Phys. 74:1367–1372.
  Article CAS Google Scholar
• Netzker, R., Köchel, H. G., Basak, N., and Küntzel, H., 1982, Nucleotide sequence of Aspergillus nidulans mitochondrial genes coding for ATPase subunit 6, cytochrome oxidase subunit 3, seven unidentified proteins, four tRNAs and L-RNA, Nucl. Acid Res. 10:4783–4794.
  Article CAS Google Scholar
• Ohnishi, T., Blum, H., Leigh, J. S., Jr., and Salerno, J. C., 1979, Membrane Bioenergetics (C. P. Lee, G. Schatz, and L. Ernster, eds.), Addison-Wesley, Reading, Massachusetts, pp. 21–30.
  Google Scholar
• Ohnishi, T., LoBrutto, R., Salerno, J. C., Bruckner, R. C., and Frey, T. G., 1982, Spatial relationship between cytochrome a and a 3, J. Biol. Chem. 257:14821–14825.
  PubMed CAS Google Scholar
• Peisach, J., 1978, EPR probes of cytochrome c oxidase, in Frontiers of Biological Energetics, Vol. 2 (P. L. Dutton J. S. Leigh, and A. Scarpa, eds.), Academic Press, New York, pp. 873–881.
  Google Scholar
• Penttilä, T., 1984, Properties and reconstitution of a subunit Ill-deficient cytochrome oxidase, Eur. J. Biochem., in press.
  Google Scholar
• Penttilä, T., and Wikström, M., 1981, Mechanism of proton/electron coupling in cytochrome oxidase, in: Vectorial Reactions in Electron and Ion Transport in Mitochondria and Bacteria (F. Palmieri, E. Quagliarelli, N. Siliprandi, and E. C. Slater, eds.), Elsevier/North-Holland Biomedical Press, Amsterdam, pp. 71–80.
  Google Scholar
• Perutz, M. F., Kendrew, J. C., and Watson, H. C., 1965, Structure and function of haemoglobin. II. Some relations between polypeptide chain configuration and amino acid sequence, J. Mol. Biol. 13:669–678.
  Article CAS Google Scholar
• Powers, L., Blumberg, W. E., Chance, B., Barlow, C. H., Leigh, J. S., Jr., Smith, J., Yonetani, T., Vik, S., and Peisach, J., 1979, The nature of the copper atoms of cytochrome c oxidase as studied by optical and X-ray absorption edge spectroscopy, Biochim. Biophys. Acta 546:520–538.
  Article PubMed CAS Google Scholar
• Powers, L., Chance, B., Ching, Y., and Angiolillo, P., 1981, Structural features and the reaction mechanism of cytochrome oxidase, Biophys. J. 34:465–498.
  Article PubMed CAS Google Scholar
• Poyton, R. O., and Schatz, G., 1975, Cytochrome c oxidase from baker’s yeast. III. Physical characterization of isolated subunits and chemical evidence for two different classes of polypeptides, J. Biol. Chem. 250:752–761.
  PubMed CAS Google Scholar
• Prochaska, L. J., Bisson, R., Capaldi, R. A., Steffens, G. C. M., and Buse, G., 1981, Inhibition of cytochrome c oxidation function by dicyclohexylcarbodiimide, Biochim. Biophys. Acta 637:360–373.
  Article PubMed CAS Google Scholar
• Rieder, R., and Bosshard, H. R., 1980, Comparison of the binding sites on cytochrome c for cytochrome c oxidase, cytochrome bc 1, and cytochrome c 1. Differential acetylation of lysyl residues in free and complexed cytochrome c, J. Biol. Chem. 255:4732–4739.
  PubMed CAS Google Scholar
• Ryden, L., and Lundgren, J.-O., 1976, Homology relationships among the small blue proteins, Nature 261:344–346.
  Article PubMed CAS Google Scholar
• Saari, H., Penttilä, T., and Wikström, M., 1980, Interaction of Ca2+ and H+ with heme A in cytochrome oxidase, J. Bioenerg. Biomembr. 12:325–338.
  Article PubMed CAS Google Scholar
• Sacher, R., Steffens, G. J., and Buse, G., 1979, Studies on cytochrome c oxidase. VI. Polypeptide IV— The complete primary structure, Hoppe-Seyler’s Z. Physiol. Chem. 360:1385–1392.
  Article PubMed CAS Google Scholar
• Saraste, M., 1984, How complex is a respiratory complex? TIBS, in press.
  Google Scholar
• Saraste, M., Penttilä, T., and Wikström, M., 1981, Quaternary structure of bovine cytochrome oxidase, Eur. J. Biochem. 115:261–268.
  Article PubMed CAS Google Scholar
• Scott, R. A., Cramer, S. P., Shaw, R. W., Beinert, H., and Gray, H. B., 1981, Extended X-ray absorption fine structure of copper in cytochrome c oxidase: Direct evidence for copper-sulfur ligation, Proc. Natl. Acad. Sci. USA 78:664–667.
  Article PubMed CAS Google Scholar
• Sebald, W., Machleidt, W., and Wächter, E., 1980, _N,N’_-Dicyclohexylcarbodiimide binds specifically to a single glutamyl residue of the proteolipid subunit of the mitochondrial adenosinetriphosphatases from Neurospora crassa and Saccharomyces cerevisiae, Proc. Natl. Acad. Sci. USA 77:785–789.
  Article PubMed CAS Google Scholar
• Seiter, C. H. A., Angelos, S. G., Jr., and Perreault, R. A., 1978, Resonance Raman and EPR studies of cytochrome oxidase ligand complexes, in: Frontiers of Biological Energetics, Vol. 2 (P. L. Dutton, J. S. Leigh, Jr., and A. Scarpa, eds.), Academic Press, New York, pp. 897–903.
  Google Scholar
• Shaw, R. W., Rife, J. E., O’Leary, M. H., and Beinert, H., 1981, Oxidation of reduced cytochrome c oxidase with 18O2, J. Biol. Chem. 256:1105–1107.
  PubMed CAS Google Scholar
• Smith, H. T., Ahmed, A. J., and Millet, F., 1981, Electrostatic interaction of cytochrome c with cytochrome c 1 and cytochrome oxidase, J. Biol. Chem. 256:4984–4990.
  PubMed CAS Google Scholar
• Solioz, M., Carafoli, E., and Ludwig, B., 1982, The cytochrome c oxidase of Paracoccus denitrificans pumps protons in a reconstituted system, J. Biol. Chem. 257:1579–1582.
  PubMed CAS Google Scholar
• Sone, N., and Hinkle, P. C., 1982, Proton transport by cytochrome oxidase from the thermophilic bacterium PS3 reconstituted in liposomes, J. Biol. Chem. 257:12600–12604.
  PubMed CAS Google Scholar
• Sone, N., and Yanagita, Y., 1982, A cytochrome aa 3-type terminal oxidase of a thermophilic bacterium. Purification, properties and proton pumping, Biochim. Biophys. Acta 682:216–226.
  Article CAS Google Scholar
• Steffens, G. J., and Buse, G., 1979, Studies on cytochrome c oxidase, IV. Primary structure and function of subunit II, Hoppe-Seyler’s Z. Physiol. Chem. 360:613–619.
  PubMed CAS Google Scholar
• Steffens, G. C. M., Steffens, G. J., and Buse, G., 1979, Studies on cytochrome c oxidase, VIII. The amino acid sequence of polypeptide VII, Hoppe-Seyler’s Z. Physiol. Chem. 360:1641–1650.
  Article PubMed CAS Google Scholar
• Stevens, T. H., and Chan, S. I., 1981, Histidine is the axial ligand to cytochrome a 3 in cytochrome c oxidase, J. Biol. Chem. 256:1069–1071.
  PubMed CAS Google Scholar
• Stevens, T. H., Martin, C. T., Wang, H., Brudvig, G. W., Scholes, C. P., and Chan, S. I., 1982, The nature of CuA in cytochrome c oxidase, J. Biol. Chem. 257:12106–12113.
  PubMed CAS Google Scholar
• Tanaka, M., Haniu, M., Yasunobu, K. T., Yu, C.-A., Yu, L., Wei, Y.-H., and King, T. E., 1979, Amino acid sequence of subunit V of bovine heart cytochrome oxidase, the heme _a_-containing subunit, J. Biol. Chem. 254:3879–3885.
  PubMed CAS Google Scholar
• Tanaka, M., Yasunobu, K. T., Wei, Y.-H., and King, T. E., 1981, Complete amino acid sequence of bovine heart cytochrome oxidase subunit VI, J. Biol. Chem. 256:4832–4837.
  PubMed CAS Google Scholar
• Thalenfeld, B. E., and Tzagoloff, A., 1980, Assembly of the mitochondrial membrane system. Sequence of the Oxi 2 gene of yeast mitochondrial DNA, J. Biol. Chem. 255:6173–6180.
  PubMed CAS Google Scholar
• Tweedle, M. F., Wilson, L. J., Garcia-Iniquez, L., Babcock, G. T., and Palmer, G., 1978, Electronic state of heme in cytochrome oxidase III. The magnetic susceptibility of beef heart cytochrome oxidase and some of its derivatives from 7-200K. Direct evidence for an antiferromagnetically coupled Fe(III)/ Cu(II) pair, J. Biol. Chem. 253:8065–8071.
  PubMed CAS Google Scholar
• Tzagoloff, A., 1982, Mitochondria, Plenum Press, New York and London.
  Google Scholar
• Vanderkooi, J. M., Landesberg, R., Hayden, G. W., and Owen, C. S., 1977, Metal-free and metal-substituted cytochromes c. Use in characterization of the cytochrome c binding site, Eur. J. Biochem. 81:339–347.
  Article PubMed CAS Google Scholar
• Van Gelder, B. F., and Beinert, H., 1969, Studies of the heme components of cytochrome c oxidase by EPR spectroscopy, Biochim. Biophys. Acta 189:1–24.
  Article PubMed Google Scholar
• Van Verseveld, H. W., Krab, K., and Stouthamer, A. H., 1981, Proton pump coupled to cytochrome c oxidase in Paracoccus denitrificans, Biochim. Biophys. Acta 635:525–534.
  Article PubMed Google Scholar
• Verheul, F. E. A. M., Draijer, J. W., Muijsers, A. O., and Van Gelder, B. F., 1982, The reactivity of thiol groups in bovine heart cytochrome c oxidase towards 5,5′-dithiobis(2-nitrobenzoic acid), Biochim. Biophys. Acta 681:118–129.
  Article PubMed CAS Google Scholar
• Viola, R. E., Shaw, R. W., Ransom, S. C., and Villafranca, J. J., 1983, Solvent proton relaxation studies of cytochrome c oxidase solutions, Arch. Biochem. Biophys. 220:106–115.
  Article PubMed CAS Google Scholar
• Von Jagow, G., Engel, W. D., Schägger, H., Machleidt, W., and Machleidt, I., 1981, On the mechanism of proton translocation linked to electron transfer at energy conversion site 2, in: Vectorial Reactions in Electron and Ion Transport in Mitochondria and Bacteria (F. Palmieri, E. Quagliariello, N. Siliprandi, and E. C. Slater, eds.), Elsevier/North-Holland Biomédical Press, Amsterdam, pp. 149–161.
  Google Scholar
• Wallace, D. C., 1982, Structure and evolution of organelle genomes, Microbiol. Rev. 46:208–240.
  PubMed CAS Google Scholar
• Weiss, H., and Kolb, H. J., 1979, Isolation of mitochondrial succinate: Ubiquinone reductase, cytochrome c reductase and cytochrome c oxidase from Neurospora crassa using nonionic detergent, Eur. J. Biochem. 99:139–149.
  Article PubMed CAS Google Scholar
• Wikström, M., 1972, Energy-linked change in the redox state and absorption spectrum of cytochrome a in situ, Biochim. Biophys. Acta 283:385–390.
  Article PubMed Google Scholar
• Wikström, M., 1977, Proton pump coupled to cytochrome c oxidase in mitochondria, Nature 266:271–273.
  Article PubMed Google Scholar
• Wikström, M., 1981, Cytochrome oxidase, in: Mitochondria and Microsomes (C. P. Lee, G. Schatz, and G. Dallner, eds.), Addison-Wesley, Reading, Massachusetts, p. 249–269.
  Google Scholar
• Wikström, M., and Krab, K., 1979, Proton-pumping cytochrome c oxidase, Biochim. Biophys. Acta 549:177–222.
  Article PubMed Google Scholar
• Wikström, M., and Krab, K., 1980, Respiration-linked H+ translocation in mitochondria: Stoichiometry and mechanism, Curr. Top. Bioenerg. 10:51–101.
  Google Scholar
• Wikström, M., Harmon, H. J., Ingledew, W. J., and Chance, B., 1976, A re-evaluation of the spectral, potentiometric and energy-linked properties of cytochrome c oxidase in mitochondria, FEBS Lett. 65:259–277.
  Article PubMed Google Scholar
• Wikström, M., Krab, K., and Saraste, M., 1981a, Cytochrome Oxidase—A Synthesis, Academic Press, London.
  Google Scholar
• Wikström, M., Krab, K., and Saraste, M., 1981b, Proton-translocating cytochrome complexes, Annu. Rev. Biochem. 50:623–655.
  Article PubMed Google Scholar
• Wilson, M. T., Greenwood, C., Brunori, M., and Antonini, E., 1975, Kinetic studies on the reaction between cytochrome c oxidase and ferrocytochrome c, Biochem. J. 147:145–153.
  PubMed CAS Google Scholar
• Wilson, M. T., Lalla-Maharajh, W., Darley-Usmar, V., Bonaventura, J., Bonaventura, C., and Brunori, M., 1980, Structural and functional properties of cytochrome c oxidases isolated from sharks, J. Biol. Chem. 255:2722–2728.
  PubMed CAS Google Scholar
• Wilson, M. T., Jensen, P., Aasa, R., Malmström, B. G., and Vänngård, T., 1982, An investigation by E.P.R. and optical spectroscopy of cytochrome oxidase during turnover, Biochem. J. 203:483–492.
  PubMed CAS Google Scholar
• Winter, D. B., Bruyninckx, W. J., Foulke, F. G., Grinich, N. P., and Mason, H. S., 1980, Location of heme A on subunits I and II and Cu on subunit II of cytochrome c oxidase, J. Biol. Chem. 255:11408–11414.
  PubMed CAS Google Scholar
• Woodruff, W. H., Kessler, R. J., Ferris, N. S., Dallinger, R. F., Carter, K. R., Antalis, T. M., and Palmer, G., 1982, Modern approaches to the study of cytochrome oxidase. Resonance Raman and magnetic circular dichroism characterization of the enzyme and its derivatives, in: Advances in Chemistry Series, Vol. 201, (K. M. Kadish, ed.), American Chemical Society, pp. 625–659.
  Article CAS Google Scholar
• Yamanaka, T., Kamita, Y., and Fukumori, Y., 1981, Molecular and enzymatic properties of “cytochrome aa 3”-type terminal oxidase derived from Nitrobacter agilis, J. Biochem. (Tokyo) 89:265–273.
  CAS Google Scholar
• Yoshikawa, S., Choc, M. G., O’Toole, M. C., and Caughey, W. S., 1977, An infrared study of CO binding to heart cytochrome c oxidase and hemoglobin A, J. Biol. Chem. 252:5498–5508.
  PubMed CAS Google Scholar

Download references