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Relationship of Cytochrome caa3 from Thermus thermophilus to Other Heme- and Copper-Containing Terminal Oxidases

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The Molecular Basis of Bacterial Metabolism

Abstract

Cytochrome oxidases are a key component of the energy metabolism of most aerobic organisms from mammals to bacteria. They are the final enzyme of the membrane-associated respiratory chain responsible for converting the chemical energy of reduced substrates to a transmembrane electrochemical potential, which is used by the cell for a wide variety of energy-requiring processes. The most widely studied oxidase is the cytochrome c oxidase (cytochrome aa3 oxidase) of the mammalian mitochondrion. This complex, integral membrane protein contains 13 subunits and 4 canonical metal centers : heme centers, a and a3 ; copper centers, CuA and CuB. It is responsible for electron transfer from reduced cytochrome c to dioxygen with the concomitant reduction of dioxygen to water and the coupled vectorial transfer of protons across the mitochondrial membrane (see Chan and Li 1990; Palmer 1987 for recent reviews).

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References

  • Anderson, S., de Bruijn, Coulson, A.R., Eperon, I.C., Sanger, F. & 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 

  • Annemtiller, S. & Schäfer, G. (1989) Cytochrome aa3 from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius. FEBS Lett. 244:451–455

    Article  Google Scholar 

  • Anraku, Y. (1988) Bacterial electron transport chains. Annu. Rev. Biochem. 57:101–132

    Article  PubMed  CAS  Google Scholar 

  • Bisson, R., Steffens, G.C.M. & Buse, G. (1982a) Localization of lipid binding domain(s) 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. & Buse, G. (1982b) Mapping of the cytochrome c binding site on cytochrome c oxidase. FEBS Lett. 144:359–363

    Article  PubMed  CAS  Google Scholar 

  • Bonitz, S.G., Coruzzi, G., Thalenfeld, B.E. & Tzagoloff, A. (1980) Assembly of the mitochondrial membrane system. Structure and nucleotide sequence of the gene coding for subunit I of yeast cytochrome oxidase. J. Biol. Chem. 24:11927–11941

    Google Scholar 

  • Chan, S.I. & Li, P.M. (1990) Cytochrome c oxidase: understanding nature’s design of a proton pump. Biochemistry 29:1–12

    Article  PubMed  CAS  Google Scholar 

  • Chepuri, V., Lemieux, L., Au, D.C.T. & Gennis, R.B. (1990) The Sequence of the cyo Operon Indicates Substantial Structural Similarities between the Cytochrome o Ubiquinol Oxidase of Escherichia coli and the aa 3-type Family of Cytochrome c Oxidases. J. Biol. Chem. 265:11185–11192

    PubMed  CAS  Google Scholar 

  • Clary, D.O. & Wolstenholme, D.R. (1983a) Nucleotide sequence of a segment of Drosophila mitochondrial DNA that contains the genes for cytochrome c oxidase subunits II and III and ATPase subunit 6. Nucleic Acids Res. 11:4211–4227

    Article  PubMed  CAS  Google Scholar 

  • Clary, D.O. & Wolstenholme, D.R. (1983b) Genes for cytochrome c oxidase subunit I, urf2, and 3 tRNA’s in Drosophila mitochondrial DNA. Nucleic Acids Res. 11:6859–6872

    Article  PubMed  CAS  Google Scholar 

  • Coruzzi, G. & 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 

  • Dayhoff, M.O., Schwartz, R.M. & Orcutt, B.C. (1978) A model of evolutionary change in proteins. In: Dayhoff, M.O. (ed) Atlas of protein sequence and structure, vol. 5, suppl. 3. National Biomedical Research Foundation, Washington, D.C., pp. 345–352

    Google Scholar 

  • Degli Esposti, M., Ghelli, A., Luchetti, R., Crimi, M. & Lenaz, G. (1989) New approaches to the prediction of the folding of membrane proteins with redox function. Ital. J. Biochem. 38:1–22

    PubMed  CAS  Google Scholar 

  • Devereux, J., Haeberli, P. & Smithies, O. (1984) A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res 12:387–395

    Article  PubMed  CAS  Google Scholar 

  • Doolittle, R.F. (1981) Similar amino acid sequences: chance or common ancestry? Science 214:149–159

    Article  PubMed  CAS  Google Scholar 

  • Doolittle, R.F. (1986) Of urfs and orfs. A primer on how to analyze derived amino acid sequences. University Science Books, Mill Valley, California

    Google Scholar 

  • Einarsdöttir, O., Killough, P.M., Fee, J.A. & Woodruff, W.H. (1989) An infrared study of the binding and photodissociation of carbon monoxide in cytochrome ba3 from Thermus thermophilus. J. Biol. Chem. 264:2405–2408

    PubMed  Google Scholar 

  • Fee, J.A., Kuila, D., Mather, M.W. & Yoshida, T. (1986) Respiratory proteins from extremely thermophilic, aerobic bacteria. Biochim. Biophys. Acta 853:153–185

    PubMed  CAS  Google Scholar 

  • Fee, J.A., Mather, M.W., Springer, P., Hensel, S. & Buse, G. (1988) Isolation and partial sequence of the A-protein gene of Thermus thermophilus cytochrome q aa3. Ann. New York Acad. Sci. 550:33–38

    Article  CAS  Google Scholar 

  • Gelles, J., Blair, D.F. & Chan, S.I. (1986) The proton-pumping site of cytochrome c oxidase: a model of its structure and mechanism. Biochim. Biophys. Acta 853:205–236

    PubMed  CAS  Google Scholar 

  • Gribskov, M., McLachlan, A.D. & Eisenberg, D. (1987) Profile analysis: detection of distantly related proteins. Proc. Natl. Acad. Sci. USA 84:4355–4358

    Article  PubMed  CAS  Google Scholar 

  • Hata, A., Kirino, Y., Matsuura, K., Itoh, S., Hiyama, T., Konishi, K., Kita, K. & Anraku, Y. (1985) Assignment of ESR signals of Escherichia coli terminal oxidase complexes. Biochim. Biophys. Acta 810:62–72

    Article  PubMed  CAS  Google Scholar 

  • Holm, L., Saraste, M. & Wikström, M. (1987) Structural models of the redox centres in cytochrome oxidase. EMBO J. 6:2819–2823

    PubMed  CAS  Google Scholar 

  • Hon-nami, K. & Oshima, T. (1984) Purification and characterization of cytochrome c oxidase from Thermus thermophilus HB8. Biochemistry 23:454–460

    Article  CAS  Google Scholar 

  • Ishizuka, M., Machida, K., Shimada, I. & Sone, N. (1990) (submitted)

    Google Scholar 

  • Kita, K., Konishi, K. & Anraku, Y. (1984) Terminal oxidases of Escherichia coli aerobic respiratory chain. J. Biol. Chem. 259:3368–3374

    PubMed  CAS  Google Scholar 

  • Kyte, J. & 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 

  • Martin, C.T., Scholes, C.P. & Chan, S.I. (1988) On the nature of cysteine coordination to CuA in cytochrome c oxidase. J. Biol. Chem 263:8420–8429

    PubMed  CAS  Google Scholar 

  • Mather, M.W. (1988) Base composition-independent hybridization in dried agarose gels: screening and recovery for cloning of genomic DNA fragments. Bio Techniques 6:444–447

    CAS  Google Scholar 

  • Mather, M.W., Springer, P., & Fee, J.A. (1990) (submitted)

    Google Scholar 

  • Michel, H., Weyer, K.A., Gruenberg, H., Dünger, I., Oesterhelt, D. & Lottspeich, F. (1986) The ‘light’ and ‘medium’ subunits of the photosynthetic reaction centre from Rhodospeudomonas viridis: isolation of the genes, nucleotide and amino acid sequence. EMBO J. 5:1149–1158

    PubMed  CAS  Google Scholar 

  • Millet, F., de Jong, C., Paulson, L. & Capaldi, R.A. (1983) Identification of specific carboxylate groups on cytochrome c oxidase that are involved in binding cytochrome c. Biochemistry 22:546–552

    Article  Google Scholar 

  • Müller, M., Schläpfer, B. & Azzi, A. (1988a) Preparation of a one-subunit cytochrome oxidase from Paracoccus denitrificans: spectral analysis and enzymatic activity. Biochemistry 27:7546–7551

    Article  PubMed  Google Scholar 

  • Müller, M., SchJäpfer, B. & Azzi, A. (1988b) Cytochrome c oxidase from Paracoccus denitrificans: both hemes are located in subunit I. Proc. Natl. Acad. Sci. USA 85:6647–6651

    Article  PubMed  Google Scholar 

  • Palmer, G. (1987) Cytochrome oxidase: a perspective. Pure Appl. Chem. 59:749–758

    Article  CAS  Google Scholar 

  • Puustinen, A., Finel, M., Virkki, M. & Wikström, M. (1989) Cytochrome o (bo) is a proton pump in Paracoccus denitrificans and Escherichia coli. FEBS Lett. 249:163–167

    Article  PubMed  CAS  Google Scholar 

  • Raitio, M., Tuulikki, J. & Saraste, M. (1987) Isolation and analysis of the genes for cytochrome c oxidase in Paracoccus denitrificans. EMBO J. 6:2825–2833

    PubMed  CAS  Google Scholar 

  • Robillard, G.T. & Lolkema, J.S. (1988) Enzymes II of the phosphoeno/pyruvate-dependent sugar transport systems: a review of their structure and mechanism of sugar transport. Biochim. Biophys. Acta 947:493–519

    PubMed  CAS  Google Scholar 

  • Salerno, J.C., Bolgiano, B. & Ingledew, W.J. (1989) Potentiometrie titration of cytochrome-bo type quinol oxidase of Escherichia coli: evidence for heme-heme and copper-heme interaction. FEBS Lett. 247:101–105

    Article  PubMed  CAS  Google Scholar 

  • Sanger, F., Nicklen, S. & Coulson, A.R. (1977) DNA sequencing with chain terminating inhibitors. Proc. Natl. Acad. USA 74:5463–5467

    Article  CAS  Google Scholar 

  • Saraste, M., Raitio, M., Tuulikki, J. & Perämaa, A. (1986) A gene in Paracoccus for subunit III of cytochrome oxidase. FEBS Lett. 206:154–156

    Article  PubMed  CAS  Google Scholar 

  • Sone, N., Yanagita, Y., Hon-Nami, K., Fukumori, Y. & Yamanaka, T. (1983) Proton-pump activity of Nitrobacter agilis and Thermus thermophilus cytochrome c oxidases. FEBS Lett 155:150–154

    Article  CAS  Google Scholar 

  • Sone, N., Yokoi, F., Fu, T., Ohta, S., Metso, T., Raitio, M. & Saraste, M. (1988) Nucleotide sequence of the gene coding for cytochrome oxidase subunit I from the thermophilic bacterium PS3. J. Biochem. (Tokyo) 103:606–610

    CAS  Google Scholar 

  • Steffens, G.J. & 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

    CAS  Google Scholar 

  • Steinrücke, P., Steffens, G.C.M., Panskus, G., Buse, G. & Ludwig, B. (1987) Subunit II of cytochrome c oxidase from Paracoccus denitrificans. DNA sequence, gene expression and the protein. Eur. J. Biochem. 167:431–439

    Article  PubMed  Google Scholar 

  • Sweet, R.M. & Eisenberg, D. (1983) Correlation of sequence hydrophobicities measures similarity in three-dimensional protein structures. J. Mol. Biol. 171:479–488

    Article  PubMed  CAS  Google Scholar 

  • Thalenfeld, B.E. & Tzagoloff, A. (1980) Assembly of the mitochondrial membrane system. Sequence of the Oxi2 gene of yeast mitochondrial DNA. J. Biol. Chem. 255:6173–6180

    PubMed  CAS  Google Scholar 

  • Wikström, M., Saraste, M. & Pentillä, T. (1985) Relationships between structure and function in cytochrome oxidase. In: Martonosi, A.M. (ed) The enzymes of biological membranes, vol. 4. Plenum, New York

    Google Scholar 

  • Woese, C.R. (1987) Bacterial evolution. Microbiol. Rev. 51:221–271

    PubMed  CAS  Google Scholar 

  • Yoshida, T. & Fee, J.A. (1984) Studies on cytochrome c oxidase activity of the cytochrome c1aa3 complex from Thermus thermophilus. J. Biol. Chem. 529:1031–1036

    Google Scholar 

  • Yoshida, T., Lorence, R.M., Choc, M.G., Tarr, G.E., Findling, K.L. & Fee, J.A. (1984) Respiratory proteins from the extremely thermophilic aerobic bacterium, Thermus thermophilus. J. Biol. Chem. 259:112–123

    PubMed  CAS  Google Scholar 

  • Zimmermann, B.H., Nitsche, C.I., Fee, J.A., Rusnak, F. & Münck, E. (1988) Properties of a copper-containing cytochrome ba3: a second terminal oxidase from the extreme thermophile Thermus thermophilus. Proc. Natl. Acad. Sci. USA 85:5779–5783

    Article  PubMed  CAS  Google Scholar 

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Authors and Affiliations

  1. Biochemistry Section and Stable Isotope Resource, Isotope and Structural Chemistry Group, Los Alamos National Laboratory, 87545, Los Alamos, NM, USA

    J. A. Fee

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  1. M. W. Mather
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  2. P. Springer
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  3. J. A. Fee
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Editors and Affiliations

  1. FB Biologie, Institut für Botanik, Universitätsstraße 31, W-8400, Regensburg, Germany

    Günter Hauska

  2. Laboratorium für Mikrobiologie FB Biologie, Philipps-Universität, Karl-von-Frisch-Straße, W-3500, Marburg, Germany

    Rudolf K. Thauer

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© 1990 Springer-Verlag Berlin Heidelberg

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Mather, M.W., Springer, P., Fee, J.A. (1990). Relationship of Cytochrome caa3 from Thermus thermophilus to Other Heme- and Copper-Containing Terminal Oxidases. In: Hauska, G., Thauer, R.K. (eds) The Molecular Basis of Bacterial Metabolism. 41. Colloquium der Gesellschaft für Biologische Chemie 5.–7. April 1990 in Mosbach/Baden, vol 41. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-75969-7_10

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  • DOI: https://doi.org/10.1007/978-3-642-75969-7_10

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-75971-0

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