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Purification and characterization of sulfide dehydrogenase from alkaliphilic chemolithoautotrophic sulfur-oxidizing bacteria
Extracts of the alkaliphilic sulfur-oxidizing autotroph strain AL3 contained sulfide:cytochrome c oxidoreductase. This was active above pH 8, and was associated with the cell membranes. Although up to 60% of the initial activity was lost during Triton X-100 extraction, further purification resulted...
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Published in: | FEBS letters 1998-05, Vol.427 (1), p.11-14 |
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creator | Sorokin, Dimitry Yu de Jong, Govardus A.H Robertson, Lesley A Kuenen, Gijs J |
description | Extracts of the alkaliphilic sulfur-oxidizing autotroph strain AL3 contained sulfide:cytochrome
c oxidoreductase. This was active above pH 8, and was associated with the cell membranes. Although up to 60% of the initial activity was lost during Triton X-100 extraction, further purification resulted in an enzyme that catalyzed sulfide oxidation with horse heart cytochrome
c. This enzyme was a 41 kDa protein containing heme
c
554. The optimum pH of the membrane bound enzyme was 9.0, but after extraction this fell to 8.0. The enzyme catalyzed a single electron oxidation of HS
−. Hydrosulfide radical is therefore the most probable product. |
doi_str_mv | 10.1016/S0014-5793(98)00379-2 |
format | article |
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c oxidoreductase. This was active above pH 8, and was associated with the cell membranes. Although up to 60% of the initial activity was lost during Triton X-100 extraction, further purification resulted in an enzyme that catalyzed sulfide oxidation with horse heart cytochrome
c. This enzyme was a 41 kDa protein containing heme
c
554. The optimum pH of the membrane bound enzyme was 9.0, but after extraction this fell to 8.0. The enzyme catalyzed a single electron oxidation of HS
−. Hydrosulfide radical is therefore the most probable product.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/S0014-5793(98)00379-2</identifier><identifier>PMID: 9613590</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Alkaliphilic thiobacillus ; Cytochrome c Group - isolation & purification ; Membrane protein ; Oxidation-Reduction ; Oxidoreductases - isolation & purification ; Sulfide dehydrogenase ; Sulfides - metabolism ; Sulfur metabolism ; Thiobacillus - enzymology ; Thiobacillus - metabolism ; Thiosulfate ; Thiosulfates - metabolism</subject><ispartof>FEBS letters, 1998-05, Vol.427 (1), p.11-14</ispartof><rights>1998 Federation of European Biochemical Societies</rights><rights>FEBS Letters 427 (1998) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5382-33ad9ba1d4cb82726ad0bcddbfda3496ac2a9c499e62d5d340e1d6fddcbed6fc3</citedby><cites>FETCH-LOGICAL-c5382-33ad9ba1d4cb82726ad0bcddbfda3496ac2a9c499e62d5d340e1d6fddcbed6fc3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0014579398003792$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3548,27923,27924,45779</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9613590$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sorokin, Dimitry Yu</creatorcontrib><creatorcontrib>de Jong, Govardus A.H</creatorcontrib><creatorcontrib>Robertson, Lesley A</creatorcontrib><creatorcontrib>Kuenen, Gijs J</creatorcontrib><title>Purification and characterization of sulfide dehydrogenase from alkaliphilic chemolithoautotrophic sulfur-oxidizing bacteria</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Extracts of the alkaliphilic sulfur-oxidizing autotroph strain AL3 contained sulfide:cytochrome
c oxidoreductase. This was active above pH 8, and was associated with the cell membranes. Although up to 60% of the initial activity was lost during Triton X-100 extraction, further purification resulted in an enzyme that catalyzed sulfide oxidation with horse heart cytochrome
c. This enzyme was a 41 kDa protein containing heme
c
554. The optimum pH of the membrane bound enzyme was 9.0, but after extraction this fell to 8.0. The enzyme catalyzed a single electron oxidation of HS
−. Hydrosulfide radical is therefore the most probable product.</description><subject>Alkaliphilic thiobacillus</subject><subject>Cytochrome c Group - isolation & purification</subject><subject>Membrane protein</subject><subject>Oxidation-Reduction</subject><subject>Oxidoreductases - isolation & purification</subject><subject>Sulfide dehydrogenase</subject><subject>Sulfides - metabolism</subject><subject>Sulfur metabolism</subject><subject>Thiobacillus - enzymology</subject><subject>Thiobacillus - metabolism</subject><subject>Thiosulfate</subject><subject>Thiosulfates - metabolism</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><recordid>eNqNkEtv1DAQxy1EVbaFj1ApJwSHgB95-YSgailSpVYCzpbjmXQHknixE-hW_fDkseoVTiPP_zHWj7Ezwd8JLor3XzkXWZqXWr3R1VvOValT-YxtRFWqVGVF9Zxtniwv2EmMP_j0roQ-Zse6ECrXfMMeb8dADTk7kO8T20PitjZYN2Cgh3XpmySObUOACeB2D8HfYW8jJk3wXWLbn7al3ZZaclMWO9_SsPV2HPwQ_LR3S3oMqb8noAfq75J67bcv2VFj24ivDvOUfb-8-HZ-lV7ffP5y_vE6dbmqZKqUBV1bAZmrK1nKwgKvHUDdgFWZLqyTVrtMaywk5KAyjgKKBsDVOE2nTtnrtXcX_K8R42A6ig7b1vbox2hKrbmWlZyM-Wp0wccYsDG7QJ0NeyO4mambhbqZkRpdmYW6mXNnhwNj3SE8pQ6YJ_1q1f9Qi_v_KzWXF5_kosyCrpb1fOrDWoUTsN-EwURH2DsECugGA57-8dm_rnKrmw</recordid><startdate>19980501</startdate><enddate>19980501</enddate><creator>Sorokin, Dimitry Yu</creator><creator>de Jong, Govardus A.H</creator><creator>Robertson, Lesley A</creator><creator>Kuenen, Gijs J</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</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>19980501</creationdate><title>Purification and characterization of sulfide dehydrogenase from alkaliphilic chemolithoautotrophic sulfur-oxidizing bacteria</title><author>Sorokin, Dimitry Yu ; de Jong, Govardus A.H ; Robertson, Lesley A ; Kuenen, Gijs J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5382-33ad9ba1d4cb82726ad0bcddbfda3496ac2a9c499e62d5d340e1d6fddcbed6fc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Alkaliphilic thiobacillus</topic><topic>Cytochrome c Group - isolation & purification</topic><topic>Membrane protein</topic><topic>Oxidation-Reduction</topic><topic>Oxidoreductases - isolation & purification</topic><topic>Sulfide dehydrogenase</topic><topic>Sulfides - metabolism</topic><topic>Sulfur metabolism</topic><topic>Thiobacillus - enzymology</topic><topic>Thiobacillus - metabolism</topic><topic>Thiosulfate</topic><topic>Thiosulfates - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sorokin, Dimitry Yu</creatorcontrib><creatorcontrib>de Jong, Govardus A.H</creatorcontrib><creatorcontrib>Robertson, Lesley A</creatorcontrib><creatorcontrib>Kuenen, Gijs J</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sorokin, Dimitry Yu</au><au>de Jong, Govardus A.H</au><au>Robertson, Lesley A</au><au>Kuenen, Gijs J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and characterization of sulfide dehydrogenase from alkaliphilic chemolithoautotrophic sulfur-oxidizing bacteria</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1998-05-01</date><risdate>1998</risdate><volume>427</volume><issue>1</issue><spage>11</spage><epage>14</epage><pages>11-14</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>Extracts of the alkaliphilic sulfur-oxidizing autotroph strain AL3 contained sulfide:cytochrome
c oxidoreductase. This was active above pH 8, and was associated with the cell membranes. Although up to 60% of the initial activity was lost during Triton X-100 extraction, further purification resulted in an enzyme that catalyzed sulfide oxidation with horse heart cytochrome
c. This enzyme was a 41 kDa protein containing heme
c
554. The optimum pH of the membrane bound enzyme was 9.0, but after extraction this fell to 8.0. The enzyme catalyzed a single electron oxidation of HS
−. Hydrosulfide radical is therefore the most probable product.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>9613590</pmid><doi>10.1016/S0014-5793(98)00379-2</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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language | eng |
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subjects | Alkaliphilic thiobacillus Cytochrome c Group - isolation & purification Membrane protein Oxidation-Reduction Oxidoreductases - isolation & purification Sulfide dehydrogenase Sulfides - metabolism Sulfur metabolism Thiobacillus - enzymology Thiobacillus - metabolism Thiosulfate Thiosulfates - metabolism |
title | Purification and characterization of sulfide dehydrogenase from alkaliphilic chemolithoautotrophic sulfur-oxidizing bacteria |
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