Identification of cytochrome c oxidase in the alkaliphilic, obligately chemolithoautotrophic, sulfur-oxidizing bacterium ‘Thioalcalomicrobium aerophilum’ strain AL 3
Abstract Cytochrome c oxidase from the novel alkaliphilic autotrophic sulfur bacterium ‘Thioalcalomicrobium aerophilum’ strain AL 3 was isolated and purified 87-fold. Spectroscopic analysis revealed the presence of both c- and b-type hemes as well as copper in a ratio of 3:2:1. The purified enzyme c...
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| Veröffentlicht in: | FEMS microbiology letters 1999-10, Vol.179 (1), p.91-99 |
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| creator | Sorokin, Dimitry Yu Cherepanov, Alexei de Vries, Simon Kuenen, Gijs J. |
| description | Abstract
Cytochrome c oxidase from the novel alkaliphilic autotrophic sulfur bacterium ‘Thioalcalomicrobium aerophilum’ strain AL 3 was isolated and purified 87-fold. Spectroscopic analysis revealed the presence of both c- and b-type hemes as well as copper in a ratio of 3:2:1. The purified enzyme consists of three subunits with apparent molecular masses of 41, 34 and 32 kDa. The two small subunits contain covalently bound heme c. With TMPD as a substrate the pH optimum was determined to be pH 8.0. In the presence of monovalent cations the specific activity of the purified oxidase increased significantly. The enzyme was not able to oxidize external cytochrome c, but accepted electron from its native electron donor. The latter was separated from the other membrane cytochromes during anion-exchange chromatography and was identified as a high potential cytochrome c551. Overall the data indicate that the cytochrome c oxidase from this alkaliphilic autotrophic bacterium belongs to the heme-copper oxidase superfamily; regarding its subunit composition and content of prosthetic groups, the enzyme is similar in many aspects to the cbb3-type cytochrome c oxidases described for several neutrophilic bacteria, including anaerobic phototrophic and aerobic sulfur-oxidizing bacteria. |
| doi_str_mv | 10.1111/j.1574-6968.1999.tb08713.x |
| format | Article |
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Cytochrome c oxidase from the novel alkaliphilic autotrophic sulfur bacterium ‘Thioalcalomicrobium aerophilum’ strain AL 3 was isolated and purified 87-fold. Spectroscopic analysis revealed the presence of both c- and b-type hemes as well as copper in a ratio of 3:2:1. The purified enzyme consists of three subunits with apparent molecular masses of 41, 34 and 32 kDa. The two small subunits contain covalently bound heme c. With TMPD as a substrate the pH optimum was determined to be pH 8.0. In the presence of monovalent cations the specific activity of the purified oxidase increased significantly. The enzyme was not able to oxidize external cytochrome c, but accepted electron from its native electron donor. The latter was separated from the other membrane cytochromes during anion-exchange chromatography and was identified as a high potential cytochrome c551. Overall the data indicate that the cytochrome c oxidase from this alkaliphilic autotrophic bacterium belongs to the heme-copper oxidase superfamily; regarding its subunit composition and content of prosthetic groups, the enzyme is similar in many aspects to the cbb3-type cytochrome c oxidases described for several neutrophilic bacteria, including anaerobic phototrophic and aerobic sulfur-oxidizing bacteria.</description><identifier>ISSN: 0378-1097</identifier><identifier>EISSN: 1574-6968</identifier><identifier>DOI: 10.1111/j.1574-6968.1999.tb08713.x</identifier><identifier>PMID: 10481092</identifier><identifier>CODEN: FMLED7</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Alkaliphilic sulfur‐oxidizing bacterium ; Anion exchanging ; Anion-exchange chromatography ; Bacteria ; Cations ; cbb3‐type oxidase ; Copper ; Cytochrome ; Cytochrome c oxidase ; Cytochromes ; Enzymes ; Heme ; Leukocytes (neutrophilic) ; Microbiology ; Oxidase ; Oxidation ; pH effects ; Prostheses ; Prosthetic groups ; Substrates ; Subunit structure ; Sulfur</subject><ispartof>FEMS microbiology letters, 1999-10, Vol.179 (1), p.91-99</ispartof><rights>1999 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved. 1999</rights><rights>1999 INIST-CNRS</rights><rights>1999 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3211-4dd276fa77fac1a545c763389c31edd6ac1d2c02aff4caee3264b9d3be20337f3</citedby><cites>FETCH-LOGICAL-c3211-4dd276fa77fac1a545c763389c31edd6ac1d2c02aff4caee3264b9d3be20337f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1574-6968.1999.tb08713.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1574-6968.1999.tb08713.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,27924,27925,45574,45575</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=1932137$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10481092$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sorokin, Dimitry Yu</creatorcontrib><creatorcontrib>Cherepanov, Alexei</creatorcontrib><creatorcontrib>de Vries, Simon</creatorcontrib><creatorcontrib>Kuenen, Gijs J.</creatorcontrib><title>Identification of cytochrome c oxidase in the alkaliphilic, obligately chemolithoautotrophic, sulfur-oxidizing bacterium ‘Thioalcalomicrobium aerophilum’ strain AL 3</title><title>FEMS microbiology letters</title><addtitle>FEMS Microbiol Lett</addtitle><description>Abstract
Cytochrome c oxidase from the novel alkaliphilic autotrophic sulfur bacterium ‘Thioalcalomicrobium aerophilum’ strain AL 3 was isolated and purified 87-fold. Spectroscopic analysis revealed the presence of both c- and b-type hemes as well as copper in a ratio of 3:2:1. The purified enzyme consists of three subunits with apparent molecular masses of 41, 34 and 32 kDa. The two small subunits contain covalently bound heme c. With TMPD as a substrate the pH optimum was determined to be pH 8.0. In the presence of monovalent cations the specific activity of the purified oxidase increased significantly. The enzyme was not able to oxidize external cytochrome c, but accepted electron from its native electron donor. The latter was separated from the other membrane cytochromes during anion-exchange chromatography and was identified as a high potential cytochrome c551. Overall the data indicate that the cytochrome c oxidase from this alkaliphilic autotrophic bacterium belongs to the heme-copper oxidase superfamily; regarding its subunit composition and content of prosthetic groups, the enzyme is similar in many aspects to the cbb3-type cytochrome c oxidases described for several neutrophilic bacteria, including anaerobic phototrophic and aerobic sulfur-oxidizing bacteria.</description><subject>Alkaliphilic sulfur‐oxidizing bacterium</subject><subject>Anion exchanging</subject><subject>Anion-exchange chromatography</subject><subject>Bacteria</subject><subject>Cations</subject><subject>cbb3‐type oxidase</subject><subject>Copper</subject><subject>Cytochrome</subject><subject>Cytochrome c oxidase</subject><subject>Cytochromes</subject><subject>Enzymes</subject><subject>Heme</subject><subject>Leukocytes (neutrophilic)</subject><subject>Microbiology</subject><subject>Oxidase</subject><subject>Oxidation</subject><subject>pH effects</subject><subject>Prostheses</subject><subject>Prosthetic groups</subject><subject>Substrates</subject><subject>Subunit structure</subject><subject>Sulfur</subject><issn>0378-1097</issn><issn>1574-6968</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqVkcFu1DAQhiMEotvCKyALOHAgwY6TOEHiUFUUKi3iUs7WxLEbL0682I7Y5dTHKI_Aa_VJcMgKEIIDvlgaf__M7_mT5DHBGYnnxSYjJSvSqqnqjDRNk4UW14zQbHcnWf18upusMGV1SnDDjpJj7zcY4yLH1f3kiOCijvV8lXy76OQYtNICgrYjsgqJfbCid3aQSCC70x14ifSIQi8RmI9g9LbXRovnyLZGX0GQZo9ELwdrdOgtTMEGZyMTCT8ZNbl07qK_6PEKtSCCdHoa0O31zWWvLRgBxg5aONvOZZA_tGYabq-_Ih8cxNGna0QfJPcUGC8fHu6T5MP568uzt-n6_ZuLs9N1KmhOSFp0Xc4qBYwpEATKohSsorRuBCWy66pY7HKBc1CqECAlzauibTrayhxTyhQ9SZ4tfbfOfpqkD3zQXkhjYJR28pzUZUMJxrSO6JM_0I2d3Bjd8ZwSwsq4ZxaplwsVv-i9k4pvnR7A7TnBfA6Ub_icGp9T43Og_BAo30Xxo8OIqR1k95t0STACTw8A-LhJ5WAU2v_imrgVOpt4tWCftZH7_3DAz9-tGxL15aK30_Yf6vRv_r8DqjbTfw</recordid><startdate>199910</startdate><enddate>199910</enddate><creator>Sorokin, Dimitry Yu</creator><creator>Cherepanov, Alexei</creator><creator>de Vries, Simon</creator><creator>Kuenen, Gijs J.</creator><general>Blackwell Publishing Ltd</general><general>Blackwell</general><general>Oxford University Press</general><scope>IQODW</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QL</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>199910</creationdate><title>Identification of cytochrome c oxidase in the alkaliphilic, obligately chemolithoautotrophic, sulfur-oxidizing bacterium ‘Thioalcalomicrobium aerophilum’ strain AL 3</title><author>Sorokin, Dimitry Yu ; 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Cytochrome c oxidase from the novel alkaliphilic autotrophic sulfur bacterium ‘Thioalcalomicrobium aerophilum’ strain AL 3 was isolated and purified 87-fold. Spectroscopic analysis revealed the presence of both c- and b-type hemes as well as copper in a ratio of 3:2:1. The purified enzyme consists of three subunits with apparent molecular masses of 41, 34 and 32 kDa. The two small subunits contain covalently bound heme c. With TMPD as a substrate the pH optimum was determined to be pH 8.0. In the presence of monovalent cations the specific activity of the purified oxidase increased significantly. The enzyme was not able to oxidize external cytochrome c, but accepted electron from its native electron donor. The latter was separated from the other membrane cytochromes during anion-exchange chromatography and was identified as a high potential cytochrome c551. Overall the data indicate that the cytochrome c oxidase from this alkaliphilic autotrophic bacterium belongs to the heme-copper oxidase superfamily; regarding its subunit composition and content of prosthetic groups, the enzyme is similar in many aspects to the cbb3-type cytochrome c oxidases described for several neutrophilic bacteria, including anaerobic phototrophic and aerobic sulfur-oxidizing bacteria.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>10481092</pmid><doi>10.1111/j.1574-6968.1999.tb08713.x</doi><tpages>9</tpages></addata></record> |
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| identifier | ISSN: 0378-1097 |
| ispartof | FEMS microbiology letters, 1999-10, Vol.179 (1), p.91-99 |
| issn | 0378-1097 1574-6968 |
| language | eng |
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| source | Access via Wiley Online Library; Oxford University Press Journals All Titles (1996-Current); Alma/SFX Local Collection |
| subjects | Alkaliphilic sulfur‐oxidizing bacterium Anion exchanging Anion-exchange chromatography Bacteria Cations cbb3‐type oxidase Copper Cytochrome Cytochrome c oxidase Cytochromes Enzymes Heme Leukocytes (neutrophilic) Microbiology Oxidase Oxidation pH effects Prostheses Prosthetic groups Substrates Subunit structure Sulfur |
| title | Identification of cytochrome c oxidase in the alkaliphilic, obligately chemolithoautotrophic, sulfur-oxidizing bacterium ‘Thioalcalomicrobium aerophilum’ strain AL 3 |
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