Fast Electron Transfer from Cytochrome c6 and Plastocyanin to Photosystem I of Chlamydomonas reinhardtii Requires PsaF
To study the function of the PsaF subunit of photosystem I (PSI), the interactions between plastocyanin or cytochrome c6 and PSI isolated from wild-type and a PsaF-deficient mutant of Chlamydomonas reinhardtii have been examined using cross-linking techniques and flash absorption spectroscopy. We sh...
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| Veröffentlicht in: | Biochemistry (Easton) 1997-05, Vol.36 (21), p.6343-6349 |
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| container_end_page | 6349 |
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| container_issue | 21 |
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| container_title | Biochemistry (Easton) |
| container_volume | 36 |
| creator | HIPPLER, Michael DREPPER, Friedel FARAH, Joseph ROCHAIX, Jean-David |
| description | To study the function of the PsaF subunit of photosystem I (PSI), the interactions between plastocyanin or cytochrome c6 and PSI isolated from wild-type and a PsaF-deficient mutant of Chlamydomonas reinhardtii have been examined using cross-linking techniques and flash absorption spectroscopy. We show that efficient electron transfer from both plastocyanin and cytochrome c6 to PSI depends on PsaF. A remarkable feature of the PSI complex of C. reinhardtii is that both plastocyanin and cytochrome c6 reduce P700+ with first-order kinetics and a half-time of 3 micros, which is unique among photosynthetic organisms examined. |
| doi_str_mv | 10.1021/bi970082c |
| format | Article |
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We show that efficient electron transfer from both plastocyanin and cytochrome c6 to PSI depends on PsaF. A remarkable feature of the PSI complex of C. reinhardtii is that both plastocyanin and cytochrome c6 reduce P700+ with first-order kinetics and a half-time of 3 micros, which is unique among photosynthetic organisms examined.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi970082c</identifier><identifier>PMID: 9174349</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Animals ; Chlamydomonas reinhardtii - genetics ; Chlamydomonas reinhardtii - metabolism ; Cross-Linking Reagents ; Cytochromes - metabolism ; Cytochromes f ; Electron Transport ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; Membrane Proteins - physiology ; Mutation ; Oxidation-Reduction ; Photosynthetic Reaction Center Complex Proteins - genetics ; Photosynthetic Reaction Center Complex Proteins - isolation & purification ; Photosynthetic Reaction Center Complex Proteins - metabolism ; Photosystem I Protein Complex ; Plastocyanin - metabolism ; Protozoan Proteins</subject><ispartof>Biochemistry (Easton), 1997-05, Vol.36 (21), p.6343-6349</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27923,27924</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9174349$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>HIPPLER, Michael</creatorcontrib><creatorcontrib>DREPPER, Friedel</creatorcontrib><creatorcontrib>FARAH, Joseph</creatorcontrib><creatorcontrib>ROCHAIX, Jean-David</creatorcontrib><title>Fast Electron Transfer from Cytochrome c6 and Plastocyanin to Photosystem I of Chlamydomonas reinhardtii Requires PsaF</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>To study the function of the PsaF subunit of photosystem I (PSI), the interactions between plastocyanin or cytochrome c6 and PSI isolated from wild-type and a PsaF-deficient mutant of Chlamydomonas reinhardtii have been examined using cross-linking techniques and flash absorption spectroscopy. We show that efficient electron transfer from both plastocyanin and cytochrome c6 to PSI depends on PsaF. A remarkable feature of the PSI complex of C. reinhardtii is that both plastocyanin and cytochrome c6 reduce P700+ with first-order kinetics and a half-time of 3 micros, which is unique among photosynthetic organisms examined.</description><subject>Animals</subject><subject>Chlamydomonas reinhardtii - genetics</subject><subject>Chlamydomonas reinhardtii - metabolism</subject><subject>Cross-Linking Reagents</subject><subject>Cytochromes - metabolism</subject><subject>Cytochromes f</subject><subject>Electron Transport</subject><subject>Membrane Proteins - genetics</subject><subject>Membrane Proteins - metabolism</subject><subject>Membrane Proteins - physiology</subject><subject>Mutation</subject><subject>Oxidation-Reduction</subject><subject>Photosynthetic Reaction Center Complex Proteins - genetics</subject><subject>Photosynthetic Reaction Center Complex Proteins - isolation & purification</subject><subject>Photosynthetic Reaction Center Complex Proteins - metabolism</subject><subject>Photosystem I Protein Complex</subject><subject>Plastocyanin - metabolism</subject><subject>Protozoan Proteins</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kF1LwzAUhoMoc04v_AFCrryr5rNtLqVsOhAss4h3JW1TGm2bLUnF_nsDG16d8_I8HDgvALcYPWBE8GOlRYJQSuozsMScoIgJwc_BEiEUR0TE6BJcOfcVIkMJW4CFwAmjTCzBz0Y6D9e9qr01IyysHF2rLGytGWA2e1N3YVOwjqEcG5j3QTf1LEc9Qm9g3hlv3Oy8GuAWmhZmXS-HuTGDGaWDVumxk7bxWsOdOkzaKgdzJzfX4KKVvVM3p7kCxWZdZC_R69vzNnt6jTTmwkcYt7xVmNWKE0pilTLSNiEkuKoqQnnTVpghGTPB0iSoiMYVxrROU4JoQ-kK3B_P7q05TMr5ctCuVn0vR2UmVyYCxZhQFsS7kzhVg2rKvdWDtHN56inw6Mh1ePX3H0v7XcYJTXhZ5O9lzhH-ZLuPckf_ACeFeVw</recordid><startdate>19970527</startdate><enddate>19970527</enddate><creator>HIPPLER, Michael</creator><creator>DREPPER, Friedel</creator><creator>FARAH, Joseph</creator><creator>ROCHAIX, Jean-David</creator><general>American Chemical Society</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>19970527</creationdate><title>Fast Electron Transfer from Cytochrome c6 and Plastocyanin to Photosystem I of Chlamydomonas reinhardtii Requires PsaF</title><author>HIPPLER, Michael ; 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We show that efficient electron transfer from both plastocyanin and cytochrome c6 to PSI depends on PsaF. A remarkable feature of the PSI complex of C. reinhardtii is that both plastocyanin and cytochrome c6 reduce P700+ with first-order kinetics and a half-time of 3 micros, which is unique among photosynthetic organisms examined.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>9174349</pmid><doi>10.1021/bi970082c</doi><tpages>7</tpages></addata></record> |
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| ispartof | Biochemistry (Easton), 1997-05, Vol.36 (21), p.6343-6349 |
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| language | eng |
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| subjects | Animals Chlamydomonas reinhardtii - genetics Chlamydomonas reinhardtii - metabolism Cross-Linking Reagents Cytochromes - metabolism Cytochromes f Electron Transport Membrane Proteins - genetics Membrane Proteins - metabolism Membrane Proteins - physiology Mutation Oxidation-Reduction Photosynthetic Reaction Center Complex Proteins - genetics Photosynthetic Reaction Center Complex Proteins - isolation & purification Photosynthetic Reaction Center Complex Proteins - metabolism Photosystem I Protein Complex Plastocyanin - metabolism Protozoan Proteins |
| title | Fast Electron Transfer from Cytochrome c6 and Plastocyanin to Photosystem I of Chlamydomonas reinhardtii Requires PsaF |
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