A novel, anaerobically induced ferredoxin in Chlamydomonas reinhardtii
We have found the transcript of one of at least six ferredoxin encoding genes of the green alga Chlamydomonas reinhardtii, FDX5, strongly accumulating in anaerobiosis, indicating a vital role of the encoded protein in the anaerobic metabolism of the cells. According to absorption and electron parama...
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| Veröffentlicht in: | FEBS letters 2009-01, Vol.583 (2), p.325-329 |
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| creator | Jacobs, Jessica Pudollek, Susanne Hemschemeier, Anja Happe, Thomas |
| description | We have found the transcript of one of at least six ferredoxin encoding genes of the green alga
Chlamydomonas reinhardtii,
FDX5, strongly accumulating in anaerobiosis, indicating a vital role of the encoded protein in the anaerobic metabolism of the cells. According to absorption and electron paramagnetic resonance spectroscopy, Fdx5 is a plant-type [2Fe2S]-ferredoxin with a redox potential similar to that of the ferredoxin PetF. However, although Fdx5 seems to be located in the chloroplast, it is not able to photoreduce nicotinamide adenine dinucleotide phosphate (NADP
+) via ferredoxin-NADP-reductase, nor to be an electron donor to the plastidic [FeFe]-hydrogenase HydA1. Thus, Fdx5 seems to have a special role in a yet to be identified anaerobic pathway. |
| doi_str_mv | 10.1016/j.febslet.2008.12.018 |
| format | Article |
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Chlamydomonas reinhardtii,
FDX5, strongly accumulating in anaerobiosis, indicating a vital role of the encoded protein in the anaerobic metabolism of the cells. According to absorption and electron paramagnetic resonance spectroscopy, Fdx5 is a plant-type [2Fe2S]-ferredoxin with a redox potential similar to that of the ferredoxin PetF. However, although Fdx5 seems to be located in the chloroplast, it is not able to photoreduce nicotinamide adenine dinucleotide phosphate (NADP
+) via ferredoxin-NADP-reductase, nor to be an electron donor to the plastidic [FeFe]-hydrogenase HydA1. Thus, Fdx5 seems to have a special role in a yet to be identified anaerobic pathway.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/j.febslet.2008.12.018</identifier><identifier>PMID: 19101555</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>aa(s) ; alternative oxidase ; amino acid(s) ; Anaerobiosis ; Animals ; Aox ; basepairs ; bps ; Chlamydomonas reinhardtii ; Chlamydomonas reinhardtii - enzymology ; Chlamydomonas reinhardtii - genetics ; Ferredoxin ; Ferredoxin-NADP Reductase - metabolism ; ferredoxin-NADPH-oxidoreductase ; Ferredoxins - genetics ; Ferredoxins - metabolism ; Fnr ; forward ; Green alga ; Hydrogen metabolism ; large subunit of Rubisco ; NADP ; nicotinamide adenine dinucleotide phosphate ; open reading frame ; orf ; Oxidation-Reduction ; Oxidoreductases - metabolism ; Pfl ; photosystem II, photosytem I ; PSII, PSI ; pyruvate formate lyase ; qPCR ; quantitative RealTime PCR ; ribulosebisphosphate carboxylase/oxygenase ; RNA, Messenger - biosynthesis ; Rubisco ; Rubisco LS ; S-adenosylmethionine ; SAM ; Transcription, Genetic</subject><ispartof>FEBS letters, 2009-01, Vol.583 (2), p.325-329</ispartof><rights>2008 Federation of European Biochemical Societies</rights><rights>FEBS Letters 583 (2009) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c572X-3b22ee544bf7483aa1f708939f700da4735ab289b8146cc0dfee8af775b3b3813</citedby><cites>FETCH-LOGICAL-c572X-3b22ee544bf7483aa1f708939f700da4735ab289b8146cc0dfee8af775b3b3813</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2Fj.febslet.2008.12.018$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S001457930800999X$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,1411,1427,3537,27901,27902,45550,45551,46384,46808,65534</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19101555$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Jacobs, Jessica</creatorcontrib><creatorcontrib>Pudollek, Susanne</creatorcontrib><creatorcontrib>Hemschemeier, Anja</creatorcontrib><creatorcontrib>Happe, Thomas</creatorcontrib><title>A novel, anaerobically induced ferredoxin in Chlamydomonas reinhardtii</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>We have found the transcript of one of at least six ferredoxin encoding genes of the green alga
Chlamydomonas reinhardtii,
FDX5, strongly accumulating in anaerobiosis, indicating a vital role of the encoded protein in the anaerobic metabolism of the cells. According to absorption and electron paramagnetic resonance spectroscopy, Fdx5 is a plant-type [2Fe2S]-ferredoxin with a redox potential similar to that of the ferredoxin PetF. However, although Fdx5 seems to be located in the chloroplast, it is not able to photoreduce nicotinamide adenine dinucleotide phosphate (NADP
+) via ferredoxin-NADP-reductase, nor to be an electron donor to the plastidic [FeFe]-hydrogenase HydA1. Thus, Fdx5 seems to have a special role in a yet to be identified anaerobic pathway.</description><subject>aa(s)</subject><subject>alternative oxidase</subject><subject>amino acid(s)</subject><subject>Anaerobiosis</subject><subject>Animals</subject><subject>Aox</subject><subject>basepairs</subject><subject>bps</subject><subject>Chlamydomonas reinhardtii</subject><subject>Chlamydomonas reinhardtii - enzymology</subject><subject>Chlamydomonas reinhardtii - genetics</subject><subject>Ferredoxin</subject><subject>Ferredoxin-NADP Reductase - metabolism</subject><subject>ferredoxin-NADPH-oxidoreductase</subject><subject>Ferredoxins - genetics</subject><subject>Ferredoxins - metabolism</subject><subject>Fnr</subject><subject>forward</subject><subject>Green alga</subject><subject>Hydrogen metabolism</subject><subject>large subunit of Rubisco</subject><subject>NADP</subject><subject>nicotinamide adenine dinucleotide phosphate</subject><subject>open reading frame</subject><subject>orf</subject><subject>Oxidation-Reduction</subject><subject>Oxidoreductases - metabolism</subject><subject>Pfl</subject><subject>photosystem II, photosytem I</subject><subject>PSII, PSI</subject><subject>pyruvate formate lyase</subject><subject>qPCR</subject><subject>quantitative RealTime PCR</subject><subject>ribulosebisphosphate carboxylase/oxygenase</subject><subject>RNA, Messenger - biosynthesis</subject><subject>Rubisco</subject><subject>Rubisco LS</subject><subject>S-adenosylmethionine</subject><subject>SAM</subject><subject>Transcription, Genetic</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkc1qGzEUhUVpady0j5Awq646U_2MRtKqJCZuCoEumkB2Qj93iIxmlEq2U799ZWzoMl1dJL57JL6D0AXBHcFk-LruRrAlwqajGMuO0A4T-QYtiBSsZf0g36IFxqRvuVDsDH0oZY3rWRL1Hp0RVTM45wu0umrmtIP4pTGzgZxscCbGfRNmv3XgmxFyBp_-hLleNcunaKa9T1OaTWkyhPnJZL8J4SN6N5pY4NNpnqOH1c398ra9-_n9x_LqrnVc0MeWWUoBeN_bUfSSGUNGgaViqg7sTS8YN5ZKZSXpB-ewHwGkGYXgllkmCTtHn4-5zzn93kLZ6CkUBzGaGdK26GGQbJBEvApSTAfM6VBBfgRdTqVkGPVzDpPJe02wPpjWa30yrQ-mNaG6aqx7l6cHtnYC_2_rpLYCt0fgJUTY_1-qXt1c01-H2g6tYYmxUuqxRn07RkFVuwuQdXEB5tpPyOA22qfwym__Ah0Wp2I</recordid><startdate>20090122</startdate><enddate>20090122</enddate><creator>Jacobs, Jessica</creator><creator>Pudollek, Susanne</creator><creator>Hemschemeier, Anja</creator><creator>Happe, Thomas</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>8FD</scope><scope>F1W</scope><scope>FR3</scope><scope>H95</scope><scope>L.G</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20090122</creationdate><title>A novel, anaerobically induced ferredoxin in Chlamydomonas reinhardtii</title><author>Jacobs, Jessica ; Pudollek, Susanne ; Hemschemeier, Anja ; Happe, Thomas</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c572X-3b22ee544bf7483aa1f708939f700da4735ab289b8146cc0dfee8af775b3b3813</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>aa(s)</topic><topic>alternative oxidase</topic><topic>amino acid(s)</topic><topic>Anaerobiosis</topic><topic>Animals</topic><topic>Aox</topic><topic>basepairs</topic><topic>bps</topic><topic>Chlamydomonas reinhardtii</topic><topic>Chlamydomonas reinhardtii - enzymology</topic><topic>Chlamydomonas reinhardtii - genetics</topic><topic>Ferredoxin</topic><topic>Ferredoxin-NADP Reductase - metabolism</topic><topic>ferredoxin-NADPH-oxidoreductase</topic><topic>Ferredoxins - genetics</topic><topic>Ferredoxins - metabolism</topic><topic>Fnr</topic><topic>forward</topic><topic>Green alga</topic><topic>Hydrogen metabolism</topic><topic>large subunit of Rubisco</topic><topic>NADP</topic><topic>nicotinamide adenine dinucleotide phosphate</topic><topic>open reading frame</topic><topic>orf</topic><topic>Oxidation-Reduction</topic><topic>Oxidoreductases - metabolism</topic><topic>Pfl</topic><topic>photosystem II, photosytem I</topic><topic>PSII, PSI</topic><topic>pyruvate formate lyase</topic><topic>qPCR</topic><topic>quantitative RealTime PCR</topic><topic>ribulosebisphosphate carboxylase/oxygenase</topic><topic>RNA, Messenger - biosynthesis</topic><topic>Rubisco</topic><topic>Rubisco LS</topic><topic>S-adenosylmethionine</topic><topic>SAM</topic><topic>Transcription, Genetic</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jacobs, Jessica</creatorcontrib><creatorcontrib>Pudollek, Susanne</creatorcontrib><creatorcontrib>Hemschemeier, Anja</creatorcontrib><creatorcontrib>Happe, Thomas</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>Technology Research Database</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Engineering Research Database</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Jacobs, Jessica</au><au>Pudollek, Susanne</au><au>Hemschemeier, Anja</au><au>Happe, Thomas</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A novel, anaerobically induced ferredoxin in Chlamydomonas reinhardtii</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2009-01-22</date><risdate>2009</risdate><volume>583</volume><issue>2</issue><spage>325</spage><epage>329</epage><pages>325-329</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>We have found the transcript of one of at least six ferredoxin encoding genes of the green alga
Chlamydomonas reinhardtii,
FDX5, strongly accumulating in anaerobiosis, indicating a vital role of the encoded protein in the anaerobic metabolism of the cells. According to absorption and electron paramagnetic resonance spectroscopy, Fdx5 is a plant-type [2Fe2S]-ferredoxin with a redox potential similar to that of the ferredoxin PetF. However, although Fdx5 seems to be located in the chloroplast, it is not able to photoreduce nicotinamide adenine dinucleotide phosphate (NADP
+) via ferredoxin-NADP-reductase, nor to be an electron donor to the plastidic [FeFe]-hydrogenase HydA1. Thus, Fdx5 seems to have a special role in a yet to be identified anaerobic pathway.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>19101555</pmid><doi>10.1016/j.febslet.2008.12.018</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | aa(s) alternative oxidase amino acid(s) Anaerobiosis Animals Aox basepairs bps Chlamydomonas reinhardtii Chlamydomonas reinhardtii - enzymology Chlamydomonas reinhardtii - genetics Ferredoxin Ferredoxin-NADP Reductase - metabolism ferredoxin-NADPH-oxidoreductase Ferredoxins - genetics Ferredoxins - metabolism Fnr forward Green alga Hydrogen metabolism large subunit of Rubisco NADP nicotinamide adenine dinucleotide phosphate open reading frame orf Oxidation-Reduction Oxidoreductases - metabolism Pfl photosystem II, photosytem I PSII, PSI pyruvate formate lyase qPCR quantitative RealTime PCR ribulosebisphosphate carboxylase/oxygenase RNA, Messenger - biosynthesis Rubisco Rubisco LS S-adenosylmethionine SAM Transcription, Genetic |
| title | A novel, anaerobically induced ferredoxin in Chlamydomonas reinhardtii |
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