Binuclear centre structure of terminal protonmotive oxidases
The recent proliferation of data obtained from mutant forms of cytochrome oxidase and analogous enzymes has necessitated a re-examination of existing structural models. A new model is proposed, consistent with these data, which brings several protonatable residues (Y244, D298, D300, T309, T316, K319...
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| Veröffentlicht in: | FEBS Letters 1993-02, Vol.316 (3), p.216-223 |
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| container_title | FEBS Letters |
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| creator | Brown, Simon Moody, A.John Mitchell, Roy Rich, Peter R. |
| description | The recent proliferation of data obtained from mutant forms of cytochrome oxidase and analogous enzymes has necessitated a re-examination of existing structural models. A new model is proposed, consistent with these data, which brings several protonatable residues (Y244, D298, D300, T309, T316, K319, T326) into the vicinity of the binuclear centre, suggestive of a proton-transferring function. In addition, we also consider those residues which may participate in electron transport between Cu
A and haem
a. We suggest several potential lines of investigation. |
| doi_str_mv | 10.1016/0014-5793(93)81296-C |
| format | Article |
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A and haem
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A and haem
a. We suggest several potential lines of investigation.</description><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Bacterial Proteins - chemistry</subject><subject>Biological and medical sciences</subject><subject>Biophysical Phenomena</subject><subject>Biophysics</subject><subject>Catalysis</subject><subject>Cattle</subject><subject>Cytochrome b Group - chemistry</subject><subject>Cytochrome bo</subject><subject>Cytochrome c oxidase</subject><subject>Electron Transport</subject><subject>Electron Transport Complex IV - chemistry</subject><subject>Electron Transport Complex IV - metabolism</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fungal Proteins - chemistry</subject><subject>Heme - chemistry</subject><subject>Ion Channels</subject><subject>Molecular Sequence Data</subject><subject>Oxidation-Reduction</subject><subject>Oxidoreductases</subject><subject>Protein Conformation</subject><subject>Protein Structure, Tertiary</subject><subject>Protons</subject><subject>Sequence Alignment</subject><subject>Sequence conservation</subject><subject>structure</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkEtLJDEUhYM4aPv4Bwq9EBkXNeZReYEIY2HPDDS40XVIp24gUg9NqtT-95Oym16KEEhyz3dPbg5CZwT_IpiIa4xJWXCp2U_NrhShWhTVHpoRJVnBSqH20WyHHKKjlJ5xviuiD9CBFFJxLmbo5i50o2vAxrmDbogwT0Mc3TDmU-_nA8Q2dLaZv8R-6Lu2H8JbFj5CbROkE_TD2ybB6XY_Rk-L-8fqb7F8-POv-r0sXKl5VQi5Uk7W3GunSW196Zx2mHDKKFYcayo4o5QLalcl9jUlWGApfM15KbDVnh2jy41vnuJ1hDSYNiQHTWM76MdkZCa1YjyD5QZ0sU8pgjcvMbQ2rg3BZgrNTImYKRGT12dopspt51v_cdVCvWvappT1i61uk7ONj7ZzIe2wkhNJicrYYoO9hwbW33raLO7v6CRMdc0-q9M8txsjyKG-BYgmuQCdgzpEcIOp-_D1h_4DoKua0Q</recordid><startdate>19930201</startdate><enddate>19930201</enddate><creator>Brown, Simon</creator><creator>Moody, A.John</creator><creator>Mitchell, Roy</creator><creator>Rich, Peter R.</creator><general>Elsevier B.V</general><general>Elsevier</general><scope>6I.</scope><scope>AAFTH</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19930201</creationdate><title>Binuclear centre structure of terminal protonmotive oxidases</title><author>Brown, Simon ; Moody, A.John ; Mitchell, Roy ; Rich, Peter R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c495C-67b8c7d5f9c91daf4cc9c01523208509265322562ab40fd2106076fd55460a9f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Amino Acid Sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Bacterial Proteins - chemistry</topic><topic>Biological and medical sciences</topic><topic>Biophysical Phenomena</topic><topic>Biophysics</topic><topic>Catalysis</topic><topic>Cattle</topic><topic>Cytochrome b Group - chemistry</topic><topic>Cytochrome bo</topic><topic>Cytochrome c oxidase</topic><topic>Electron Transport</topic><topic>Electron Transport Complex IV - chemistry</topic><topic>Electron Transport Complex IV - metabolism</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. 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| ispartof | FEBS Letters, 1993-02, Vol.316 (3), p.216-223 |
| issn | 0014-5793 1873-3468 |
| language | eng |
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| source | Elsevier ScienceDirect Journals Complete - AutoHoldings; MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Analytical, structural and metabolic biochemistry Animals Bacterial Proteins - chemistry Biological and medical sciences Biophysical Phenomena Biophysics Catalysis Cattle Cytochrome b Group - chemistry Cytochrome bo Cytochrome c oxidase Electron Transport Electron Transport Complex IV - chemistry Electron Transport Complex IV - metabolism Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Fungal Proteins - chemistry Heme - chemistry Ion Channels Molecular Sequence Data Oxidation-Reduction Oxidoreductases Protein Conformation Protein Structure, Tertiary Protons Sequence Alignment Sequence conservation structure |
| title | Binuclear centre structure of terminal protonmotive oxidases |
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