Primary Reactions of Photosynthesis: Photoreduction of a Bound Chloroplast Ferredoxin at Low Temperature as Detected by EPR Spectroscopy
An electron paramagnetic resonance signal was observed at 25 degrees K in whole spinach chloroplasts after illumination at 77 degrees K. The light-induced epr spectrum had g-values (gx= 1.86, gy= 1.94, gz= 2.05) and a temperature dependence that were characteristic of the reduced state of a plant-ty...
Gespeichert in:
| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1971-01, Vol.68 (1), p.16-19 |
|---|---|
| Hauptverfasser: | , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 19 |
|---|---|
| container_issue | 1 |
| container_start_page | 16 |
| container_title | Proceedings of the National Academy of Sciences - PNAS |
| container_volume | 68 |
| creator | Malkin, R. Bearden, Alan J. |
| description | An electron paramagnetic resonance signal was observed at 25 degrees K in whole spinach chloroplasts after illumination at 77 degrees K. The light-induced epr spectrum had g-values (gx= 1.86, gy= 1.94, gz= 2.05) and a temperature dependence that were characteristic of the reduced state of a plant-type ferredoxin. The light-induced epr spectrum was also observed in broken spinach chloroplasts from which soluble ferredoxin was removed. Chemical analyses showed that both whole and broken spinach chloroplasts contained amounts of nonheme iron and ``acid-labile sulfide'' consistent with the presence of a bound iron-sulfur protein, at a level of about one molecule per 75 chlorophy II molecules. These results support the conclusion that chloroplasts contain a bound ferredoxin that may serve as a primary low-potential electron acceptor in photosynthesis. |
| doi_str_mv | 10.1073/pnas.68.1.16 |
| format | Article |
| fullrecord | <record><control><sourceid>jstor_pnas_</sourceid><recordid>TN_cdi_pnas_primary_68_1_16</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><jstor_id>60770</jstor_id><sourcerecordid>60770</sourcerecordid><originalsourceid>FETCH-LOGICAL-c446t-abea12c8d2fe053eb470665dde157b02c0f13741233cbf0cb548bd06015ba9103</originalsourceid><addsrcrecordid>eNp1kc1u1DAURi1EVYbCjhUIyQuWZLi2EyepxAKG_kkjMSplbdnODZMqE0e2A5034LFJyNDCgpV1dc5nW_cj5AWDJYNcvOs7HZayWLIlk4_IgkHJEpmW8JgsAHieFClPn5CnIdwCQJkVcEyOU8E5z8oF-bnxzU77Pb1GbWPjukBdTTdbF13Yd3GLoQmn8-yxGn4rk6HpRzd0FV1tW-dd3-oQ6Tn60XF3TUd1pGv3g97grkev4-CR6kA_YUQbsaJmT8821_RLP47eBev6_TNyVOs24PPDeUK-np_drC6T9eeLq9WHdWLTVMZEG9SM26LiNUIm0KQ5SJlVFbIsN8At1EzkKeNCWFODNVlamAoksMzokoE4Ie_ne_vB7LCy2EWvW9XPa1BON-pf0jVb9c19V6KcNjvm3855O348eKzvowzU1Iea-lCyUEwxOeqv_37uXj4UMPJXBz6l_tCH9Jv_U1UPbRvxLo7ay1m7DWNNDx7kOYhfwN6qbw</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>Primary Reactions of Photosynthesis: Photoreduction of a Bound Chloroplast Ferredoxin at Low Temperature as Detected by EPR Spectroscopy</title><source>MEDLINE</source><source>JSTOR Archive Collection A-Z Listing</source><source>PubMed Central</source><source>Alma/SFX Local Collection</source><source>Free Full-Text Journals in Chemistry</source><creator>Malkin, R. ; Bearden, Alan J.</creator><creatorcontrib>Malkin, R. ; Bearden, Alan J.</creatorcontrib><description>An electron paramagnetic resonance signal was observed at 25 degrees K in whole spinach chloroplasts after illumination at 77 degrees K. The light-induced epr spectrum had g-values (gx= 1.86, gy= 1.94, gz= 2.05) and a temperature dependence that were characteristic of the reduced state of a plant-type ferredoxin. The light-induced epr spectrum was also observed in broken spinach chloroplasts from which soluble ferredoxin was removed. Chemical analyses showed that both whole and broken spinach chloroplasts contained amounts of nonheme iron and ``acid-labile sulfide'' consistent with the presence of a bound iron-sulfur protein, at a level of about one molecule per 75 chlorophy II molecules. These results support the conclusion that chloroplasts contain a bound ferredoxin that may serve as a primary low-potential electron acceptor in photosynthesis.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.68.1.16</identifier><identifier>PMID: 4322259</identifier><language>eng</language><publisher>United States: National Academy of Sciences of the United States of America</publisher><subject>Biological Sciences: Biochemistry ; Chlorophylls ; Chloroplasts ; Chloroplasts - metabolism ; Chloroplasts - radiation effects ; Cold Temperature ; Electron Spin Resonance Spectroscopy ; Electrons ; Ferredoxins ; Ferredoxins - radiation effects ; Light ; Magnetic fields ; Molecules ; Photochemistry ; Photosynthesis ; Plant Proteins - radiation effects ; Plants ; Plants, Edible - cytology ; Radiation Effects ; Spinach ; Sulfides ; Sulfides - analysis ; Sulfites</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1971-01, Vol.68 (1), p.16-19</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c446t-abea12c8d2fe053eb470665dde157b02c0f13741233cbf0cb548bd06015ba9103</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/68/1.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/60770$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/60770$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,727,780,784,803,885,27924,27925,53791,53793,58017,58250</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/4322259$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Malkin, R.</creatorcontrib><creatorcontrib>Bearden, Alan J.</creatorcontrib><title>Primary Reactions of Photosynthesis: Photoreduction of a Bound Chloroplast Ferredoxin at Low Temperature as Detected by EPR Spectroscopy</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>An electron paramagnetic resonance signal was observed at 25 degrees K in whole spinach chloroplasts after illumination at 77 degrees K. The light-induced epr spectrum had g-values (gx= 1.86, gy= 1.94, gz= 2.05) and a temperature dependence that were characteristic of the reduced state of a plant-type ferredoxin. The light-induced epr spectrum was also observed in broken spinach chloroplasts from which soluble ferredoxin was removed. Chemical analyses showed that both whole and broken spinach chloroplasts contained amounts of nonheme iron and ``acid-labile sulfide'' consistent with the presence of a bound iron-sulfur protein, at a level of about one molecule per 75 chlorophy II molecules. These results support the conclusion that chloroplasts contain a bound ferredoxin that may serve as a primary low-potential electron acceptor in photosynthesis.</description><subject>Biological Sciences: Biochemistry</subject><subject>Chlorophylls</subject><subject>Chloroplasts</subject><subject>Chloroplasts - metabolism</subject><subject>Chloroplasts - radiation effects</subject><subject>Cold Temperature</subject><subject>Electron Spin Resonance Spectroscopy</subject><subject>Electrons</subject><subject>Ferredoxins</subject><subject>Ferredoxins - radiation effects</subject><subject>Light</subject><subject>Magnetic fields</subject><subject>Molecules</subject><subject>Photochemistry</subject><subject>Photosynthesis</subject><subject>Plant Proteins - radiation effects</subject><subject>Plants</subject><subject>Plants, Edible - cytology</subject><subject>Radiation Effects</subject><subject>Spinach</subject><subject>Sulfides</subject><subject>Sulfides - analysis</subject><subject>Sulfites</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1971</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kc1u1DAURi1EVYbCjhUIyQuWZLi2EyepxAKG_kkjMSplbdnODZMqE0e2A5034LFJyNDCgpV1dc5nW_cj5AWDJYNcvOs7HZayWLIlk4_IgkHJEpmW8JgsAHieFClPn5CnIdwCQJkVcEyOU8E5z8oF-bnxzU77Pb1GbWPjukBdTTdbF13Yd3GLoQmn8-yxGn4rk6HpRzd0FV1tW-dd3-oQ6Tn60XF3TUd1pGv3g97grkev4-CR6kA_YUQbsaJmT8821_RLP47eBev6_TNyVOs24PPDeUK-np_drC6T9eeLq9WHdWLTVMZEG9SM26LiNUIm0KQ5SJlVFbIsN8At1EzkKeNCWFODNVlamAoksMzokoE4Ie_ne_vB7LCy2EWvW9XPa1BON-pf0jVb9c19V6KcNjvm3855O348eKzvowzU1Iea-lCyUEwxOeqv_37uXj4UMPJXBz6l_tCH9Jv_U1UPbRvxLo7ay1m7DWNNDx7kOYhfwN6qbw</recordid><startdate>19710101</startdate><enddate>19710101</enddate><creator>Malkin, R.</creator><creator>Bearden, Alan J.</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</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>5PM</scope></search><sort><creationdate>19710101</creationdate><title>Primary Reactions of Photosynthesis: Photoreduction of a Bound Chloroplast Ferredoxin at Low Temperature as Detected by EPR Spectroscopy</title><author>Malkin, R. ; Bearden, Alan J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c446t-abea12c8d2fe053eb470665dde157b02c0f13741233cbf0cb548bd06015ba9103</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1971</creationdate><topic>Biological Sciences: Biochemistry</topic><topic>Chlorophylls</topic><topic>Chloroplasts</topic><topic>Chloroplasts - metabolism</topic><topic>Chloroplasts - radiation effects</topic><topic>Cold Temperature</topic><topic>Electron Spin Resonance Spectroscopy</topic><topic>Electrons</topic><topic>Ferredoxins</topic><topic>Ferredoxins - radiation effects</topic><topic>Light</topic><topic>Magnetic fields</topic><topic>Molecules</topic><topic>Photochemistry</topic><topic>Photosynthesis</topic><topic>Plant Proteins - radiation effects</topic><topic>Plants</topic><topic>Plants, Edible - cytology</topic><topic>Radiation Effects</topic><topic>Spinach</topic><topic>Sulfides</topic><topic>Sulfides - analysis</topic><topic>Sulfites</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Malkin, R.</creatorcontrib><creatorcontrib>Bearden, Alan J.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Malkin, R.</au><au>Bearden, Alan J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Primary Reactions of Photosynthesis: Photoreduction of a Bound Chloroplast Ferredoxin at Low Temperature as Detected by EPR Spectroscopy</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1971-01-01</date><risdate>1971</risdate><volume>68</volume><issue>1</issue><spage>16</spage><epage>19</epage><pages>16-19</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>An electron paramagnetic resonance signal was observed at 25 degrees K in whole spinach chloroplasts after illumination at 77 degrees K. The light-induced epr spectrum had g-values (gx= 1.86, gy= 1.94, gz= 2.05) and a temperature dependence that were characteristic of the reduced state of a plant-type ferredoxin. The light-induced epr spectrum was also observed in broken spinach chloroplasts from which soluble ferredoxin was removed. Chemical analyses showed that both whole and broken spinach chloroplasts contained amounts of nonheme iron and ``acid-labile sulfide'' consistent with the presence of a bound iron-sulfur protein, at a level of about one molecule per 75 chlorophy II molecules. These results support the conclusion that chloroplasts contain a bound ferredoxin that may serve as a primary low-potential electron acceptor in photosynthesis.</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>4322259</pmid><doi>10.1073/pnas.68.1.16</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0027-8424 |
| ispartof | Proceedings of the National Academy of Sciences - PNAS, 1971-01, Vol.68 (1), p.16-19 |
| issn | 0027-8424 1091-6490 |
| language | eng |
| recordid | cdi_pnas_primary_68_1_16 |
| source | MEDLINE; JSTOR Archive Collection A-Z Listing; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Biological Sciences: Biochemistry Chlorophylls Chloroplasts Chloroplasts - metabolism Chloroplasts - radiation effects Cold Temperature Electron Spin Resonance Spectroscopy Electrons Ferredoxins Ferredoxins - radiation effects Light Magnetic fields Molecules Photochemistry Photosynthesis Plant Proteins - radiation effects Plants Plants, Edible - cytology Radiation Effects Spinach Sulfides Sulfides - analysis Sulfites |
| title | Primary Reactions of Photosynthesis: Photoreduction of a Bound Chloroplast Ferredoxin at Low Temperature as Detected by EPR Spectroscopy |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-04T22%3A08%3A45IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-jstor_pnas_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Primary%20Reactions%20of%20Photosynthesis:%20Photoreduction%20of%20a%20Bound%20Chloroplast%20Ferredoxin%20at%20Low%20Temperature%20as%20Detected%20by%20EPR%20Spectroscopy&rft.jtitle=Proceedings%20of%20the%20National%20Academy%20of%20Sciences%20-%20PNAS&rft.au=Malkin,%20R.&rft.date=1971-01-01&rft.volume=68&rft.issue=1&rft.spage=16&rft.epage=19&rft.pages=16-19&rft.issn=0027-8424&rft.eissn=1091-6490&rft_id=info:doi/10.1073/pnas.68.1.16&rft_dat=%3Cjstor_pnas_%3E60770%3C/jstor_pnas_%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_id=info:pmid/4322259&rft_jstor_id=60770&rfr_iscdi=true |