New Insight into Microbial Iron Oxidation as Revealed by the Proteomic Profile of an Obligate Iron-Oxidizing Chemolithoautotroph
Microaerophilic, neutrophilic, iron-oxidizing bacteria (FeOB) grow via the oxidation of reduced Fe(II) at or near neutral pH, in the presence of oxygen, making them relevant in numerous environments with elevated Fe(II) concentrations. However, the biochemical mechanisms for Fe(II) oxidation by thes...
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| Veröffentlicht in: | Applied and environmental microbiology 2015-09, Vol.81 (17), p.5927-5937 |
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| creator | Barco, Roman A Emerson, David Sylvan, Jason B Orcutt, Beth N Jacobson Meyers, Myrna E Ramírez, Gustavo A Zhong, John D Edwards, Katrina J |
| description | Microaerophilic, neutrophilic, iron-oxidizing bacteria (FeOB) grow via the oxidation of reduced Fe(II) at or near neutral pH, in the presence of oxygen, making them relevant in numerous environments with elevated Fe(II) concentrations. However, the biochemical mechanisms for Fe(II) oxidation by these neutrophilic FeOB are unknown, and genetic markers for this process are unavailable. In the ocean, microaerophilic microorganisms in the genus Mariprofundus of the class Zetaproteobacteria are the only organisms known to chemolithoautotrophically oxidize Fe and concurrently biomineralize it in the form of twisted stalks of iron oxyhydroxides. The aim of this study was to identify highly expressed proteins associated with the electron transport chain of microaerophilic, neutrophilic FeOB. To this end, Mariprofundus ferrooxydans PV-1 was cultivated, and its proteins were extracted, assayed for redox activity, and analyzed via liquid chromatography-tandem mass spectrometry for identification of peptides. The results indicate that a cytochrome c4, cbb3-type cytochrome oxidase subunits, and an outer membrane cytochrome c were among the most highly expressed proteins and suggest an involvement in the process of aerobic, neutrophilic bacterial Fe oxidation. Proteins associated with alternative complex III, phosphate transport, carbon fixation, and biofilm formation were abundant, consistent with the lifestyle of Mariprofundus. |
| doi_str_mv | 10.1128/AEM.01374-15 |
| format | Article |
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However, the biochemical mechanisms for Fe(II) oxidation by these neutrophilic FeOB are unknown, and genetic markers for this process are unavailable. In the ocean, microaerophilic microorganisms in the genus Mariprofundus of the class Zetaproteobacteria are the only organisms known to chemolithoautotrophically oxidize Fe and concurrently biomineralize it in the form of twisted stalks of iron oxyhydroxides. The aim of this study was to identify highly expressed proteins associated with the electron transport chain of microaerophilic, neutrophilic FeOB. To this end, Mariprofundus ferrooxydans PV-1 was cultivated, and its proteins were extracted, assayed for redox activity, and analyzed via liquid chromatography-tandem mass spectrometry for identification of peptides. The results indicate that a cytochrome c4, cbb3-type cytochrome oxidase subunits, and an outer membrane cytochrome c were among the most highly expressed proteins and suggest an involvement in the process of aerobic, neutrophilic bacterial Fe oxidation. Proteins associated with alternative complex III, phosphate transport, carbon fixation, and biofilm formation were abundant, consistent with the lifestyle of Mariprofundus.</description><identifier>ISSN: 0099-2240</identifier><identifier>EISSN: 1098-5336</identifier><identifier>DOI: 10.1128/AEM.01374-15</identifier><identifier>PMID: 26092463</identifier><identifier>CODEN: AEMIDF</identifier><language>eng</language><publisher>United States: American Society for Microbiology</publisher><subject>Bacteria ; Bacterial Proteins - chemistry ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Chemoautotrophic Growth ; Chromatography ; Geomicrobiology ; Iron - metabolism ; Mass spectrometry ; Molecular Sequence Data ; Oxidation ; Oxidation-Reduction ; Peptides ; Proteins ; Proteobacteria - chemistry ; Proteobacteria - genetics ; Proteobacteria - metabolism ; Proteomics</subject><ispartof>Applied and environmental microbiology, 2015-09, Vol.81 (17), p.5927-5937</ispartof><rights>Copyright © 2015, American Society for Microbiology. All Rights Reserved.</rights><rights>Copyright American Society for Microbiology Sep 2015</rights><rights>Copyright © 2015, American Society for Microbiology. 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Proteins associated with alternative complex III, phosphate transport, carbon fixation, and biofilm formation were abundant, consistent with the lifestyle of Mariprofundus.</description><subject>Bacteria</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>Chemoautotrophic Growth</subject><subject>Chromatography</subject><subject>Geomicrobiology</subject><subject>Iron - metabolism</subject><subject>Mass spectrometry</subject><subject>Molecular Sequence Data</subject><subject>Oxidation</subject><subject>Oxidation-Reduction</subject><subject>Peptides</subject><subject>Proteins</subject><subject>Proteobacteria - chemistry</subject><subject>Proteobacteria - genetics</subject><subject>Proteobacteria - metabolism</subject><subject>Proteomics</subject><issn>0099-2240</issn><issn>1098-5336</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkU1v1DAQhi1ERbeFG2dkiQuHpvgzsS9I1aqlK7UUIThbTjzZuErixXZKy4mfTtKWCjh5ZD9-xuMXodeUHFPK1PuT08tjQnklCiqfoRUlWhWS8_I5WhGidcGYIPvoIKVrQoggpXqB9llJNBMlX6Ffn-AH3ozJb7uM_ZgDvvRNDLW3Pd7EMOKrW-9s9nNlE_4CN2B7cLi-w7kD_DmGDGHwzVK1vgccWmznS3XvtzbDvaJYFP6nH7d43cEQep-7YKcccgy77iXaa22f4NXjeoi-nZ1-XZ8XF1cfN-uTi6IRlOVCS1Wp1lXgbF2Jmquy1NBaJSpQqmFON03rnNJgbd0KITW1UM9bVJTCWUn4Ifrw4N1N9QCugTFH25td9IONdyZYb_49GX1ntuHGCCkp49UsePcoiOH7BCmbwacG-t6OEKZkaEVYKXmlll5v_0OvwxTHebyF4lLJUsiZOnqg5v9OKUL79BhKzBKtmaM199EauuBv_h7gCf6TJf8NsA-h-w</recordid><startdate>20150901</startdate><enddate>20150901</enddate><creator>Barco, Roman A</creator><creator>Emerson, David</creator><creator>Sylvan, Jason B</creator><creator>Orcutt, Beth N</creator><creator>Jacobson Meyers, Myrna E</creator><creator>Ramírez, Gustavo A</creator><creator>Zhong, John D</creator><creator>Edwards, Katrina J</creator><general>American Society for Microbiology</general><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>7QL</scope><scope>7QO</scope><scope>7SN</scope><scope>7SS</scope><scope>7ST</scope><scope>7T7</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>SOI</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20150901</creationdate><title>New Insight into Microbial Iron Oxidation as Revealed by the Proteomic Profile of an Obligate Iron-Oxidizing Chemolithoautotroph</title><author>Barco, Roman A ; 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The results indicate that a cytochrome c4, cbb3-type cytochrome oxidase subunits, and an outer membrane cytochrome c were among the most highly expressed proteins and suggest an involvement in the process of aerobic, neutrophilic bacterial Fe oxidation. Proteins associated with alternative complex III, phosphate transport, carbon fixation, and biofilm formation were abundant, consistent with the lifestyle of Mariprofundus.</abstract><cop>United States</cop><pub>American Society for Microbiology</pub><pmid>26092463</pmid><doi>10.1128/AEM.01374-15</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Bacteria Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Chemoautotrophic Growth Chromatography Geomicrobiology Iron - metabolism Mass spectrometry Molecular Sequence Data Oxidation Oxidation-Reduction Peptides Proteins Proteobacteria - chemistry Proteobacteria - genetics Proteobacteria - metabolism Proteomics |
| title | New Insight into Microbial Iron Oxidation as Revealed by the Proteomic Profile of an Obligate Iron-Oxidizing Chemolithoautotroph |
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