Ferredoxin-thioredoxin reductase: A catalytically active dithiol group links photoreduced ferredoxin to thioredoxin functional in photosynthetic enzyme regulation
The mechanism by which the ferredoxin-thioredoxin system activates the target enzyme, NADP-malate dehydrogenase, was investigated by analyzing the sulfhydryl status of individual protein components with [ 14C]iodoacetate and monobromobimane. The data indicate that ferredoxin-thioredoxin reductase (F...
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| Veröffentlicht in: | Arch. Biochem. Biophys.; (United States) 1987-07, Vol.256 (1), p.372-380 |
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| container_title | Arch. Biochem. Biophys.; (United States) |
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| creator | Droux, M. Miginiac-Maslow, M. Jacquot, J.-P. Gadal, P. Crawford, N.A. Kosower, N.S. Buchanan, B.B. |
| description | The mechanism by which the ferredoxin-thioredoxin system activates the target enzyme, NADP-malate dehydrogenase, was investigated by analyzing the sulfhydryl status of individual protein components with [
14C]iodoacetate and monobromobimane. The data indicate that ferredoxin-thioredoxin reductase (FTR)—an iron-sulfur enzyme present in oxygenic photosynthetic organisms—is the first member of a thiol chain that links light to enzyme regulation. FTR possesses a catalytically active dithiol group localized on the 13 kDa (similar) subunit, that occurs in all species investigated and accepts reducing equivalents from photoreduced ferredoxin and transfers them stoichiometrically to the disulfide form of thioredoxin
m. The reduced thioredoxin
m, in turn, reduces NADP-malate dehydrogenase, thereby converting it from an inactive (S-S) to an active (SH) form. The means by which FTR is able to combine electrons (from photoreduced ferredoxin) with protons (from the medium) to reduce its active disulfide group remains to be determined. |
| doi_str_mv | 10.1016/0003-9861(87)90458-9 |
| format | Article |
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14C]iodoacetate and monobromobimane. The data indicate that ferredoxin-thioredoxin reductase (FTR)—an iron-sulfur enzyme present in oxygenic photosynthetic organisms—is the first member of a thiol chain that links light to enzyme regulation. FTR possesses a catalytically active dithiol group localized on the 13 kDa (similar) subunit, that occurs in all species investigated and accepts reducing equivalents from photoreduced ferredoxin and transfers them stoichiometrically to the disulfide form of thioredoxin
m. The reduced thioredoxin
m, in turn, reduces NADP-malate dehydrogenase, thereby converting it from an inactive (S-S) to an active (SH) form. The means by which FTR is able to combine electrons (from photoreduced ferredoxin) with protons (from the medium) to reduce its active disulfide group remains to be determined.</description><identifier>ISSN: 0003-9861</identifier><identifier>EISSN: 1096-0384</identifier><identifier>DOI: 10.1016/0003-9861(87)90458-9</identifier><identifier>PMID: 3606128</identifier><identifier>CODEN: ABBIA4</identifier><language>eng</language><publisher>San Diego, CA: Elsevier Inc</publisher><subject>550201 - Biochemistry- Tracer Techniques ; ALKYLATED AROMATICS ; Applied sciences ; AROMATICS ; BARYONS ; BASIC BIOLOGICAL SCIENCES ; BIOLOGICAL FUNCTIONS ; CARBON 14 COMPOUNDS ; CATALYSIS ; CHEMICAL REACTIONS ; ELECTRONS ; ELEMENTARY PARTICLES ; ENZYMES ; Exact sciences and technology ; FERMIONS ; FERREDOXIN ; Ferredoxins - analysis ; FUNCTIONS ; HADRONS ; HYDROCARBONS ; Iron-Sulfur Proteins ; ISOTOPE APPLICATIONS ; LABELLED COMPOUNDS ; LEPTONS ; Life Sciences ; Light ; Malate Dehydrogenase - radiation effects ; METALLOPROTEINS ; NUCLEONS ; ORGANIC COMPOUNDS ; Other techniques and industries ; Oxidation-Reduction - radiation effects ; OXIDOREDUCTASES ; Oxidoreductases - metabolism ; Oxidoreductases - radiation effects ; PHOTOCHEMICAL REACTIONS ; PHOTOSYNTHESIS ; PLANTS ; Plants - enzymology ; PROTEINS ; PROTONS ; REDOX REACTIONS ; Space life sciences ; STOICHIOMETRY ; Sulfhydryl Compounds - analysis ; SYNTHESIS ; Thioredoxins - analysis ; TOLUENE ; Toluene - analogs & derivatives ; Toluene - analysis ; TRACER TECHNIQUES</subject><ispartof>Arch. Biochem. Biophys.; (United States), 1987-07, Vol.256 (1), p.372-380</ispartof><rights>1987 Academic Press, Inc. All rights of reproduction in any form reserved.</rights><rights>1988 INIST-CNRS</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c447t-c12ec826d490ead55b16e824aecfdea578fc56e3ac9c8c1a893552d87bf6dfd33</citedby><cites>FETCH-LOGICAL-c447t-c12ec826d490ead55b16e824aecfdea578fc56e3ac9c8c1a893552d87bf6dfd33</cites><orcidid>0000-0003-4975-8587 ; 0000-0001-5635-2046</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0003-9861(87)90458-9$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,315,781,785,886,3551,27928,27929,45999</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7843692$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3606128$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-02321667$$DView record in HAL$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/6075597$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Droux, M.</creatorcontrib><creatorcontrib>Miginiac-Maslow, M.</creatorcontrib><creatorcontrib>Jacquot, J.-P.</creatorcontrib><creatorcontrib>Gadal, P.</creatorcontrib><creatorcontrib>Crawford, N.A.</creatorcontrib><creatorcontrib>Kosower, N.S.</creatorcontrib><creatorcontrib>Buchanan, B.B.</creatorcontrib><creatorcontrib>Universite de Paris-Sud, Orsay, France</creatorcontrib><title>Ferredoxin-thioredoxin reductase: A catalytically active dithiol group links photoreduced ferredoxin to thioredoxin functional in photosynthetic enzyme regulation</title><title>Arch. Biochem. Biophys.; (United States)</title><addtitle>Arch Biochem Biophys</addtitle><description>The mechanism by which the ferredoxin-thioredoxin system activates the target enzyme, NADP-malate dehydrogenase, was investigated by analyzing the sulfhydryl status of individual protein components with [
14C]iodoacetate and monobromobimane. The data indicate that ferredoxin-thioredoxin reductase (FTR)—an iron-sulfur enzyme present in oxygenic photosynthetic organisms—is the first member of a thiol chain that links light to enzyme regulation. FTR possesses a catalytically active dithiol group localized on the 13 kDa (similar) subunit, that occurs in all species investigated and accepts reducing equivalents from photoreduced ferredoxin and transfers them stoichiometrically to the disulfide form of thioredoxin
m. The reduced thioredoxin
m, in turn, reduces NADP-malate dehydrogenase, thereby converting it from an inactive (S-S) to an active (SH) form. The means by which FTR is able to combine electrons (from photoreduced ferredoxin) with protons (from the medium) to reduce its active disulfide group remains to be determined.</description><subject>550201 - Biochemistry- Tracer Techniques</subject><subject>ALKYLATED AROMATICS</subject><subject>Applied sciences</subject><subject>AROMATICS</subject><subject>BARYONS</subject><subject>BASIC BIOLOGICAL SCIENCES</subject><subject>BIOLOGICAL FUNCTIONS</subject><subject>CARBON 14 COMPOUNDS</subject><subject>CATALYSIS</subject><subject>CHEMICAL REACTIONS</subject><subject>ELECTRONS</subject><subject>ELEMENTARY PARTICLES</subject><subject>ENZYMES</subject><subject>Exact sciences and technology</subject><subject>FERMIONS</subject><subject>FERREDOXIN</subject><subject>Ferredoxins - analysis</subject><subject>FUNCTIONS</subject><subject>HADRONS</subject><subject>HYDROCARBONS</subject><subject>Iron-Sulfur Proteins</subject><subject>ISOTOPE APPLICATIONS</subject><subject>LABELLED COMPOUNDS</subject><subject>LEPTONS</subject><subject>Life Sciences</subject><subject>Light</subject><subject>Malate Dehydrogenase - radiation effects</subject><subject>METALLOPROTEINS</subject><subject>NUCLEONS</subject><subject>ORGANIC COMPOUNDS</subject><subject>Other techniques and industries</subject><subject>Oxidation-Reduction - radiation effects</subject><subject>OXIDOREDUCTASES</subject><subject>Oxidoreductases - metabolism</subject><subject>Oxidoreductases - radiation effects</subject><subject>PHOTOCHEMICAL REACTIONS</subject><subject>PHOTOSYNTHESIS</subject><subject>PLANTS</subject><subject>Plants - enzymology</subject><subject>PROTEINS</subject><subject>PROTONS</subject><subject>REDOX REACTIONS</subject><subject>Space life sciences</subject><subject>STOICHIOMETRY</subject><subject>Sulfhydryl Compounds - analysis</subject><subject>SYNTHESIS</subject><subject>Thioredoxins - analysis</subject><subject>TOLUENE</subject><subject>Toluene - analogs & derivatives</subject><subject>Toluene - analysis</subject><subject>TRACER TECHNIQUES</subject><issn>0003-9861</issn><issn>1096-0384</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kc2OFCEUhStGM7ajb6AJMWbiLEqhfoByYdKZOI5JJ250TWi4NY3S0ALVseZxfFKprk7FlSt-7ncO93KK4iXB7wgm9D3GuC47Tslbzq473LS87B4VK4I7WuKaN4-L1YI8LZ7F-ANjQhpaXRQXNcWUVHxV_LmFEED738aVaWf8eY_yOqgkI3xAa6RkknZMRklrRyRVMkdA2ky8RffBDwdkjfsZ0WHnkz9JQaN-cUbJo3_N-8FlD--kRfl0EsXRpR3kJxC4h3EPuYH7wcqJel486aWN8OK8Xhbfbz99u7krN18_f7lZb0rVNCyVilSgeEV102GQum23hAKvGgmq1yBbxnvVUqil6hRXRPKubttKc7btqe51XV8Wr2dfH5MRUZkEaqe8c6CSoJi1bccydD1DO2nFIZi9DKPw0oi79UZMd7iqK0IpO5LMXs3sIfhfA8Qk9iYqsFY68EMUjFFCeDuZNjOogo8xQL84EyymrMUUpJiCFJyJU9aiy7JXZ_9huwe9iM7h5vqbc13GHF0fpFMmLhjjTU27KmMfZwzy5x4NhGl2cDlCE6bRtTf_7-MvhavKkA</recordid><startdate>19870701</startdate><enddate>19870701</enddate><creator>Droux, M.</creator><creator>Miginiac-Maslow, M.</creator><creator>Jacquot, J.-P.</creator><creator>Gadal, P.</creator><creator>Crawford, N.A.</creator><creator>Kosower, N.S.</creator><creator>Buchanan, B.B.</creator><general>Elsevier Inc</general><general>Elsevier</general><scope>IQODW</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><scope>1XC</scope><scope>OTOTI</scope><orcidid>https://orcid.org/0000-0003-4975-8587</orcidid><orcidid>https://orcid.org/0000-0001-5635-2046</orcidid></search><sort><creationdate>19870701</creationdate><title>Ferredoxin-thioredoxin reductase: A catalytically active dithiol group links photoreduced ferredoxin to thioredoxin functional in photosynthetic enzyme regulation</title><author>Droux, M. ; Miginiac-Maslow, M. ; Jacquot, J.-P. ; Gadal, P. ; Crawford, N.A. ; Kosower, N.S. ; Buchanan, B.B.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c447t-c12ec826d490ead55b16e824aecfdea578fc56e3ac9c8c1a893552d87bf6dfd33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>550201 - Biochemistry- Tracer Techniques</topic><topic>ALKYLATED AROMATICS</topic><topic>Applied sciences</topic><topic>AROMATICS</topic><topic>BARYONS</topic><topic>BASIC BIOLOGICAL SCIENCES</topic><topic>BIOLOGICAL FUNCTIONS</topic><topic>CARBON 14 COMPOUNDS</topic><topic>CATALYSIS</topic><topic>CHEMICAL REACTIONS</topic><topic>ELECTRONS</topic><topic>ELEMENTARY PARTICLES</topic><topic>ENZYMES</topic><topic>Exact sciences and technology</topic><topic>FERMIONS</topic><topic>FERREDOXIN</topic><topic>Ferredoxins - analysis</topic><topic>FUNCTIONS</topic><topic>HADRONS</topic><topic>HYDROCARBONS</topic><topic>Iron-Sulfur Proteins</topic><topic>ISOTOPE APPLICATIONS</topic><topic>LABELLED COMPOUNDS</topic><topic>LEPTONS</topic><topic>Life Sciences</topic><topic>Light</topic><topic>Malate Dehydrogenase - radiation effects</topic><topic>METALLOPROTEINS</topic><topic>NUCLEONS</topic><topic>ORGANIC COMPOUNDS</topic><topic>Other techniques and industries</topic><topic>Oxidation-Reduction - radiation effects</topic><topic>OXIDOREDUCTASES</topic><topic>Oxidoreductases - metabolism</topic><topic>Oxidoreductases - radiation effects</topic><topic>PHOTOCHEMICAL REACTIONS</topic><topic>PHOTOSYNTHESIS</topic><topic>PLANTS</topic><topic>Plants - enzymology</topic><topic>PROTEINS</topic><topic>PROTONS</topic><topic>REDOX REACTIONS</topic><topic>Space life sciences</topic><topic>STOICHIOMETRY</topic><topic>Sulfhydryl Compounds - analysis</topic><topic>SYNTHESIS</topic><topic>Thioredoxins - analysis</topic><topic>TOLUENE</topic><topic>Toluene - analogs & derivatives</topic><topic>Toluene - analysis</topic><topic>TRACER TECHNIQUES</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Droux, M.</creatorcontrib><creatorcontrib>Miginiac-Maslow, M.</creatorcontrib><creatorcontrib>Jacquot, J.-P.</creatorcontrib><creatorcontrib>Gadal, P.</creatorcontrib><creatorcontrib>Crawford, N.A.</creatorcontrib><creatorcontrib>Kosower, N.S.</creatorcontrib><creatorcontrib>Buchanan, B.B.</creatorcontrib><creatorcontrib>Universite de Paris-Sud, Orsay, France</creatorcontrib><collection>Pascal-Francis</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><collection>Hyper Article en Ligne (HAL)</collection><collection>OSTI.GOV</collection><jtitle>Arch. Biochem. Biophys.; (United States)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Droux, M.</au><au>Miginiac-Maslow, M.</au><au>Jacquot, J.-P.</au><au>Gadal, P.</au><au>Crawford, N.A.</au><au>Kosower, N.S.</au><au>Buchanan, B.B.</au><aucorp>Universite de Paris-Sud, Orsay, France</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Ferredoxin-thioredoxin reductase: A catalytically active dithiol group links photoreduced ferredoxin to thioredoxin functional in photosynthetic enzyme regulation</atitle><jtitle>Arch. Biochem. Biophys.; (United States)</jtitle><addtitle>Arch Biochem Biophys</addtitle><date>1987-07-01</date><risdate>1987</risdate><volume>256</volume><issue>1</issue><spage>372</spage><epage>380</epage><pages>372-380</pages><issn>0003-9861</issn><eissn>1096-0384</eissn><coden>ABBIA4</coden><abstract>The mechanism by which the ferredoxin-thioredoxin system activates the target enzyme, NADP-malate dehydrogenase, was investigated by analyzing the sulfhydryl status of individual protein components with [
14C]iodoacetate and monobromobimane. The data indicate that ferredoxin-thioredoxin reductase (FTR)—an iron-sulfur enzyme present in oxygenic photosynthetic organisms—is the first member of a thiol chain that links light to enzyme regulation. FTR possesses a catalytically active dithiol group localized on the 13 kDa (similar) subunit, that occurs in all species investigated and accepts reducing equivalents from photoreduced ferredoxin and transfers them stoichiometrically to the disulfide form of thioredoxin
m. The reduced thioredoxin
m, in turn, reduces NADP-malate dehydrogenase, thereby converting it from an inactive (S-S) to an active (SH) form. The means by which FTR is able to combine electrons (from photoreduced ferredoxin) with protons (from the medium) to reduce its active disulfide group remains to be determined.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>3606128</pmid><doi>10.1016/0003-9861(87)90458-9</doi><tpages>9</tpages><orcidid>https://orcid.org/0000-0003-4975-8587</orcidid><orcidid>https://orcid.org/0000-0001-5635-2046</orcidid></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0003-9861 |
| ispartof | Arch. Biochem. Biophys.; (United States), 1987-07, Vol.256 (1), p.372-380 |
| issn | 0003-9861 1096-0384 |
| language | eng |
| recordid | cdi_hal_primary_oai_HAL_hal_02321667v1 |
| source | MEDLINE; Access via ScienceDirect (Elsevier) |
| subjects | 550201 - Biochemistry- Tracer Techniques ALKYLATED AROMATICS Applied sciences AROMATICS BARYONS BASIC BIOLOGICAL SCIENCES BIOLOGICAL FUNCTIONS CARBON 14 COMPOUNDS CATALYSIS CHEMICAL REACTIONS ELECTRONS ELEMENTARY PARTICLES ENZYMES Exact sciences and technology FERMIONS FERREDOXIN Ferredoxins - analysis FUNCTIONS HADRONS HYDROCARBONS Iron-Sulfur Proteins ISOTOPE APPLICATIONS LABELLED COMPOUNDS LEPTONS Life Sciences Light Malate Dehydrogenase - radiation effects METALLOPROTEINS NUCLEONS ORGANIC COMPOUNDS Other techniques and industries Oxidation-Reduction - radiation effects OXIDOREDUCTASES Oxidoreductases - metabolism Oxidoreductases - radiation effects PHOTOCHEMICAL REACTIONS PHOTOSYNTHESIS PLANTS Plants - enzymology PROTEINS PROTONS REDOX REACTIONS Space life sciences STOICHIOMETRY Sulfhydryl Compounds - analysis SYNTHESIS Thioredoxins - analysis TOLUENE Toluene - analogs & derivatives Toluene - analysis TRACER TECHNIQUES |
| title | Ferredoxin-thioredoxin reductase: A catalytically active dithiol group links photoreduced ferredoxin to thioredoxin functional in photosynthetic enzyme regulation |
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