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1Cytochrome Oxidase Genes from Thermus Thermophilus. Nucleotide Sequence and Analysis of the Deduced Primary Structure of Subunit IIc of Cytochrome Caa3.

MW MATHER,P SPRINGER, S HENSEL, G BUSE,JA FEE

Cytochrome caa3, a cytochrome c oxidase from Thermus thermophilus, has been purified and extensively characterized as a two-subunit enzyme containing the metal centers characteristic of cytochrome c oxidases (cytochromes a and a3; copper centers CuA and CuB) and an additional cytochrome c (Fee, J. A., Kuila, D., Mather, M. W., and Yoshida, T. (1986) Biochim. Biophys. Acta 853, 153-185). We have now cloned and sequenced the genes encoding the subunits of this enzyme. The smaller subunit consists of a typical oxidase subunit II sequence fused to a cytochrome c domain (Mather, M. W., Springer, P., and Fee, J. A. (1991) J. Biol. Chem. 266, 5025-5035). The larger subunit, the A-protein, is encoded by a fusion gene lying immediately downstream of the subunit IIc gene. The 5' portion of this gene encodes an oxidase subunit I homolog, whereas the 3' portion is homologous to oxidase subunits III. The A-protein from the purified enzyme appears too small from SDS-polyacrylamide gel electrophoresis and quantitative amino acid analyses to be a complete subunit I/III fusion, but it is currently not known if proteolytic processing occurs. Analyses of the sequences of oxidase subunits are presented which clearly identify T. thermophilus cytochrome caa3 as a bona fide member of the greater family of heme- and copper-requiring oxidases. As one consequence, it is confirmed that the set of invariant histidine residues (potential ligands of the metal centers) in cytochrome c oxidase subunits I and II is reduced to 8. Possible topological and helix packing models are developed based on considerations of homology, hydropathy, and variability.

1993JOURNAL OF BIOLOGICAL CHEMISTRY（1993）引用：59

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2MOLECULAR GENETIC-STUDIES OF CYTOCHROME-BA3 FROM THERMUS-THERMOPHILUS (TT) - EVIDENCE FOR A MULTISUBUNIT STRUCTURE AND HOMOLOGY TO CYTOCHROME-CAA3

JA KEIGHTLEY,MW MATHER,P SPRINGER,JA FEE,G BUSE

1992FASEB JOURNAL（1992）

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3Relationship of Cytochrome caa3 from Thermus thermophilus to Other Heme- and Copper-Containing Terminal Oxidases

M. W. Mather,P. Springer,J. A. Fee

1990The Molecular Basis of Bacterial Metabolism引用：4

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4PHYSICAL AND MOLECULAR BIOLOGICAL STUDIES ON THE TERMINAL OXIDASES OF THERMUS-THERMOPHILUS

JA FEE,MW MATHER,P SPRINGER, JA KEIGHTLEY

1990BIOLOGICAL CHEMISTRY HOPPE-SEYLER（1990）

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5Isolation and partial sequence of the A-protein gene of Thermus thermophilus cytochrome c1aa3.

J A Fee,M W Mather,P Springer,S Hensel,G Buse

Annals of the New York Academy of SciencesVolume 550, Issue 1 p. 33-38 Isolation and Partial Sequence of the A-Protein Gene of Thermus thermophilus Cytochrome c1aa3a J. A. FEE, J. A. FEE Isotope and Structural Chemistry Group Los Alamos National Laboratory Los Alamos, New Mexico 87545Search for more papers by this authorM. W. MATHER, M. W. MATHER Isotope and Structural Chemistry Group Los Alamos National Laboratory Los Alamos, New Mexico 87545Search for more papers by this authorP. SPRINGER, P. SPRINGER Isotope and Structural Chemistry Group Los Alamos National Laboratory Los Alamos, New Mexico 87545Search for more papers by this authorS. HENSEL, S. HENSEL Institut für Biochemie Fachgebiet Molekulare Biologie der Proteine Rheinisch-Westfälische Technische Hochschule Aachen 05100 Aachen, Federal Republic of GermanySearch for more papers by this authorG. BUSE, G. BUSE Institut für Biochemie Fachgebiet Molekulare Biologie der Proteine Rheinisch-Westfälische Technische Hochschule Aachen 05100 Aachen, Federal Republic of GermanySearch for more papers by this author J. A. FEE, J. A. FEE Isotope and Structural Chemistry Group Los Alamos National Laboratory Los Alamos, New Mexico 87545Search for more papers by this authorM. W. MATHER, M. W. MATHER Isotope and Structural Chemistry Group Los Alamos National Laboratory Los Alamos, New Mexico 87545Search for more papers by this authorP. SPRINGER, P. SPRINGER Isotope and Structural Chemistry Group Los Alamos National Laboratory Los Alamos, New Mexico 87545Search for more papers by this authorS. HENSEL, S. HENSEL Institut für Biochemie Fachgebiet Molekulare Biologie der Proteine Rheinisch-Westfälische Technische Hochschule Aachen 05100 Aachen, Federal Republic of GermanySearch for more papers by this authorG. BUSE, G. BUSE Institut für Biochemie Fachgebiet Molekulare Biologie der Proteine Rheinisch-Westfälische Technische Hochschule Aachen 05100 Aachen, Federal Republic of GermanySearch for more papers by this author First published: December 1988 https://doi.org/10.1111/j.1749-6632.1988.tb35319.xCitations: 12 a This work was supported by United States Public Health Service Grant GM35342 (J. A. F.) and Grant Bu 463/1 of the Deutsche Forschungsgemeinschaft (GB). AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinkedInRedditWechat Citing Literature Volume550, Issue1Cytochrome Oxidase: Structure, Function, and PhysiopathologyDecember 1988Pages 33-38 RelatedInformation

1988Annals of the New York Academy of Sciences（1988）引用：15

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6Isolation and Partial Sequence of the A-Protein Gene of Thermus thermophilus Cytochrome c<sub>1</sub>aa<sub>3</sub>

J. A. FEE,M. W. MATHER,P. SPRINGER,S. HENSEL,G. BUSE

1988ANNALS OF THE NEW YORK ACADEMY OF SCIENCES（1988）引用：15

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7Relationship of Cytochrome caa<Subscript>3</Subscript> from <Emphasis Type="Italic">Thermus thermophilus</Emphasis> to Other Heme- and Copper-Containing Terminal Oxidases

M. W. Mather,P. Springer,J. A. Fee

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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