Identification of the electron donor to flavodiiron proteins in Synechocystis sp. PCC 6803 by in vivo spectroscopy.
Identifieur interne : 000106 ( Main/Exploration ); précédent : 000105; suivant : 000107Identification of the electron donor to flavodiiron proteins in Synechocystis sp. PCC 6803 by in vivo spectroscopy.
Auteurs : Pierre Sétif [France] ; Ginga Shimakawa [Japon] ; Anja Krieger-Liszkay [France] ; Chikahiro Miyake [Japon]Source :
- Biochimica et biophysica acta. Bioenergetics [ 1879-2650 ] ; 2020.
Descripteurs français
- KwdFr :
- Cinétique (MeSH), Mutation (MeSH), NADP (métabolisme), Protéines bactériennes (génétique), Protéines bactériennes (métabolisme), Protéines à fer non hème (génétique), Protéines à fer non hème (métabolisme), Spectrométrie de fluorescence (MeSH), Synechocystis (métabolisme), Transport d'électrons (MeSH).
- MESH :
- génétique : Protéines bactériennes, Protéines à fer non hème.
- métabolisme : NADP, Protéines bactériennes, Protéines à fer non hème, Synechocystis.
- Cinétique, Mutation, Spectrométrie de fluorescence, Transport d'électrons.
English descriptors
- KwdEn :
- MESH :
- chemical , genetics : Bacterial Proteins, Nonheme Iron Proteins.
- chemical , metabolism : Bacterial Proteins, NADP, Nonheme Iron Proteins.
- metabolism : Synechocystis.
- Electron Transport, Kinetics, Mutation, Spectrometry, Fluorescence.
Abstract
Flavodiiron proteins (FDPs) of photosynthetic organisms play a photoprotective role by reducing oxygen to water and thus avoiding the accumulation of excess electrons on the photosystem I (PSI) acceptor side under stress conditions. In Synechocystis sp. PCC 6803 grown under high CO2, both FDPs Flv1 and Flv3 are indispensable for oxygen reduction. We performed a detailed in vivo kinetic study of wild-type (WT) and Δflv1/3 strains of Synechocystis using light-induced NADPH fluorescence and near-infrared absorption of iron-sulfur clusters from ferredoxin and the PSI acceptors (FAFB), collectively named FeS. These measurements were performed under conditions where the Calvin-Benson cycle is inactive or poorly activated. Under such conditions, the NADPH decay following a short illumination decays in parallel in both strains and exhibits a time lag which is correlated to the presence of reduced FeS. On the contrary, reduced FeS decays much faster in WT than in Δflv1/3 (13 vs 2 s-1). These data unambiguously show that reduced ferredoxin, or possibly reduced FAFB, is the direct electron donor to the Flv1/Flv3 heterodimer. Evidences for large reduction of (FAFB) and recombination reactions within PSI were also provided by near-infrared absorption. Mutants lacking either the NDH1-L complex, the homolog of complex I of respiration, or the Pgr5 protein show no difference with WT in the oxidation of reduced FeS following a short illumination. These observations question the participation of a significant cyclic electron flow in cyanobacteria during the first seconds of the induction phase of photosynthesis.
DOI: 10.1016/j.bbabio.2020.148256
PubMed: 32622739
Affiliations:
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Electronic address: pierre.setif@cea.fr.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Université Paris-Saclay, 91198 Gif-sur-Yvette Cedex</wicri:regionArea><placeName><region type="region" nuts="2">Île-de-France</region><settlement type="city">Gif-sur-Yvette</settlement></placeName><orgName type="university">Université Paris-Sud</orgName></affiliation></author><author><name sortKey="Shimakawa, Ginga" sort="Shimakawa, Ginga" uniqKey="Shimakawa G" first="Ginga" last="Shimakawa">Ginga Shimakawa</name><affiliation wicri:level="4"><nlm:affiliation>Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Université Paris-Saclay, 91198 Gif-sur-Yvette Cedex, France; Department of Biological and Environmental Sciences, Faculty of Agriculture, Kobe University, 1-1 Rokkodai, Nada, Kobe 657-8501, Japan; Research Center for Solar Energy Chemistry, Osaka University, 1-3 Machikaneyama, Toyonaka, Osaka 560-8631, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Université Paris-Saclay, 91198 Gif-sur-Yvette Cedex, France; Department of Biological and Environmental Sciences, Faculty of Agriculture, Kobe University, 1-1 Rokkodai, Nada, Kobe 657-8501, Japan; Research Center for Solar Energy Chemistry, Osaka University, 1-3 Machikaneyama, Toyonaka, Osaka 560-8631</wicri:regionArea><orgName type="university">Université Paris-Sud</orgName><placeName><settlement type="city">Orsay</settlement><region type="region" nuts="2">Île-de-France</region></placeName></affiliation></author><author><name sortKey="Krieger Liszkay, Anja" sort="Krieger Liszkay, Anja" uniqKey="Krieger Liszkay A" first="Anja" last="Krieger-Liszkay">Anja Krieger-Liszkay</name><affiliation wicri:level="4"><nlm:affiliation>Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Université Paris-Saclay, 91198 Gif-sur-Yvette Cedex, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Université Paris-Saclay, 91198 Gif-sur-Yvette Cedex</wicri:regionArea><placeName><region type="region" nuts="2">Île-de-France</region><settlement type="city">Gif-sur-Yvette</settlement></placeName><orgName type="university">Université Paris-Sud</orgName></affiliation></author><author><name sortKey="Miyake, Chikahiro" sort="Miyake, Chikahiro" uniqKey="Miyake C" first="Chikahiro" last="Miyake">Chikahiro Miyake</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biological and Environmental Sciences, Faculty of Agriculture, Kobe University, 1-1 Rokkodai, Nada, Kobe 657-8501, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Biological and Environmental Sciences, Faculty of Agriculture, Kobe University, 1-1 Rokkodai, Nada, Kobe 657-8501</wicri:regionArea><wicri:noRegion>Kobe 657-8501</wicri:noRegion></affiliation></author></analytic><series><title level="j">Biochimica et biophysica acta. Bioenergetics</title><idno type="eISSN">1879-2650</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Bacterial Proteins (genetics)</term><term>Bacterial Proteins (metabolism)</term><term>Electron Transport (MeSH)</term><term>Kinetics (MeSH)</term><term>Mutation (MeSH)</term><term>NADP (metabolism)</term><term>Nonheme Iron Proteins (genetics)</term><term>Nonheme Iron Proteins (metabolism)</term><term>Spectrometry, Fluorescence (MeSH)</term><term>Synechocystis (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Cinétique (MeSH)</term><term>Mutation (MeSH)</term><term>NADP (métabolisme)</term><term>Protéines bactériennes (génétique)</term><term>Protéines bactériennes (métabolisme)</term><term>Protéines à fer non hème (génétique)</term><term>Protéines à fer non hème (métabolisme)</term><term>Spectrométrie de fluorescence (MeSH)</term><term>Synechocystis (métabolisme)</term><term>Transport d'électrons (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Bacterial Proteins</term><term>Nonheme Iron Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Bacterial Proteins</term><term>NADP</term><term>Nonheme Iron Proteins</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Protéines bactériennes</term><term>Protéines à fer non hème</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Synechocystis</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>NADP</term><term>Protéines bactériennes</term><term>Protéines à fer non hème</term><term>Synechocystis</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Electron Transport</term><term>Kinetics</term><term>Mutation</term><term>Spectrometry, Fluorescence</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cinétique</term><term>Mutation</term><term>Spectrométrie de fluorescence</term><term>Transport d'électrons</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Flavodiiron proteins (FDPs) of photosynthetic organisms play a photoprotective role by reducing oxygen to water and thus avoiding the accumulation of excess electrons on the photosystem I (PSI) acceptor side under stress conditions. In Synechocystis sp. PCC 6803 grown under high CO<sub>2</sub>, both FDPs Flv1 and Flv3 are indispensable for oxygen reduction. We performed a detailed in vivo kinetic study of wild-type (WT) and Δflv1/3 strains of Synechocystis using light-induced NADPH fluorescence and near-infrared absorption of iron-sulfur clusters from ferredoxin and the PSI acceptors (F<sub>A</sub>F<sub>B</sub>), collectively named FeS. These measurements were performed under conditions where the Calvin-Benson cycle is inactive or poorly activated. Under such conditions, the NADPH decay following a short illumination decays in parallel in both strains and exhibits a time lag which is correlated to the presence of reduced FeS. On the contrary, reduced FeS decays much faster in WT than in Δflv1/3 (13 vs 2 s<sup>-1</sup>). These data unambiguously show that reduced ferredoxin, or possibly reduced F<sub>A</sub>F<sub>B</sub>, is the direct electron donor to the Flv1/Flv3 heterodimer. Evidences for large reduction of (F<sub>A</sub>F<sub>B</sub>) and recombination reactions within PSI were also provided by near-infrared absorption. Mutants lacking either the NDH1-L complex, the homolog of complex I of respiration, or the Pgr5 protein show no difference with WT in the oxidation of reduced FeS following a short illumination. These observations question the participation of a significant cyclic electron flow in cyanobacteria during the first seconds of the induction phase of photosynthesis.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">32622739</PMID><DateCompleted><Year>2020</Year><Month>10</Month><Day>26</Day></DateCompleted><DateRevised><Year>2020</Year><Month>10</Month><Day>26</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1879-2650</ISSN><JournalIssue CitedMedium="Internet"><Volume>1861</Volume><Issue>10</Issue><PubDate><Year>2020</Year><Month>10</Month><Day>01</Day></PubDate></JournalIssue><Title>Biochimica et biophysica acta. Bioenergetics</Title><ISOAbbreviation>Biochim Biophys Acta Bioenerg</ISOAbbreviation></Journal><ArticleTitle>Identification of the electron donor to flavodiiron proteins in Synechocystis sp. PCC 6803 by in vivo spectroscopy.</ArticleTitle><Pagination><MedlinePgn>148256</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0005-2728(20)30106-7</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.bbabio.2020.148256</ELocationID><Abstract><AbstractText>Flavodiiron proteins (FDPs) of photosynthetic organisms play a photoprotective role by reducing oxygen to water and thus avoiding the accumulation of excess electrons on the photosystem I (PSI) acceptor side under stress conditions. In Synechocystis sp. PCC 6803 grown under high CO<sub>2</sub>, both FDPs Flv1 and Flv3 are indispensable for oxygen reduction. We performed a detailed in vivo kinetic study of wild-type (WT) and Δflv1/3 strains of Synechocystis using light-induced NADPH fluorescence and near-infrared absorption of iron-sulfur clusters from ferredoxin and the PSI acceptors (F<sub>A</sub>F<sub>B</sub>), collectively named FeS. These measurements were performed under conditions where the Calvin-Benson cycle is inactive or poorly activated. Under such conditions, the NADPH decay following a short illumination decays in parallel in both strains and exhibits a time lag which is correlated to the presence of reduced FeS. On the contrary, reduced FeS decays much faster in WT than in Δflv1/3 (13 vs 2 s<sup>-1</sup>). These data unambiguously show that reduced ferredoxin, or possibly reduced F<sub>A</sub>F<sub>B</sub>, is the direct electron donor to the Flv1/Flv3 heterodimer. Evidences for large reduction of (F<sub>A</sub>F<sub>B</sub>) and recombination reactions within PSI were also provided by near-infrared absorption. Mutants lacking either the NDH1-L complex, the homolog of complex I of respiration, or the Pgr5 protein show no difference with WT in the oxidation of reduced FeS following a short illumination. These observations question the participation of a significant cyclic electron flow in cyanobacteria during the first seconds of the induction phase of photosynthesis.</AbstractText><CopyrightInformation>Copyright © 2020 Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Sétif</LastName><ForeName>Pierre</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Université Paris-Saclay, 91198 Gif-sur-Yvette Cedex, France. Electronic address: pierre.setif@cea.fr.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Shimakawa</LastName><ForeName>Ginga</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Université Paris-Saclay, 91198 Gif-sur-Yvette Cedex, France; Department of Biological and Environmental Sciences, Faculty of Agriculture, Kobe University, 1-1 Rokkodai, Nada, Kobe 657-8501, Japan; Research Center for Solar Energy Chemistry, Osaka University, 1-3 Machikaneyama, Toyonaka, Osaka 560-8631, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Krieger-Liszkay</LastName><ForeName>Anja</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Université Paris-Sud, Université Paris-Saclay, 91198 Gif-sur-Yvette Cedex, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Miyake</LastName><ForeName>Chikahiro</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Department of Biological and Environmental Sciences, Faculty of Agriculture, Kobe University, 1-1 Rokkodai, Nada, Kobe 657-8501, Japan.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2020</Year><Month>07</Month><Day>02</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Biochim Biophys Acta Bioenerg</MedlineTA><NlmUniqueID>101731706</NlmUniqueID><ISSNLinking>0005-2728</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001426">Bacterial Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D019159">Nonheme Iron Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>53-59-8</RegistryNumber><NameOfSubstance UI="D009249">NADP</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001426" MajorTopicYN="N">Bacterial Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004579" MajorTopicYN="N">Electron Transport</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009249" MajorTopicYN="N">NADP</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019159" MajorTopicYN="N">Nonheme Iron Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013050" MajorTopicYN="N">Spectrometry, Fluorescence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D046939" MajorTopicYN="N">Synechocystis</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Cyclic electron flow</Keyword><Keyword MajorTopicYN="Y">KLAS-NIR spectrophotometer</Keyword><Keyword MajorTopicYN="Y">NADPH fluorescence</Keyword><Keyword MajorTopicYN="Y">NDH-1L complex</Keyword><Keyword MajorTopicYN="Y">Recombination reactions</Keyword></KeywordList><CoiStatement>Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.</CoiStatement></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2020</Year><Month>03</Month><Day>24</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2020</Year><Month>06</Month><Day>19</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2020</Year><Month>06</Month><Day>19</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>7</Month><Day>6</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>10</Month><Day>27</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2020</Year><Month>7</Month><Day>6</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">32622739</ArticleId><ArticleId IdType="pii">S0005-2728(20)30106-7</ArticleId><ArticleId IdType="doi">10.1016/j.bbabio.2020.148256</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>France</li><li>Japon</li></country><region><li>Île-de-France</li></region><settlement><li>Gif-sur-Yvette</li><li>Orsay</li></settlement><orgName><li>Université Paris-Sud</li></orgName></list><tree><country name="France"><region name="Île-de-France"><name sortKey="Setif, Pierre" sort="Setif, Pierre" uniqKey="Setif P" first="Pierre" last="Sétif">Pierre Sétif</name></region><name sortKey="Krieger Liszkay, Anja" sort="Krieger Liszkay, Anja" uniqKey="Krieger Liszkay A" first="Anja" last="Krieger-Liszkay">Anja Krieger-Liszkay</name></country><country name="Japon"><region name="Île-de-France"><name sortKey="Shimakawa, Ginga" sort="Shimakawa, Ginga" uniqKey="Shimakawa G" first="Ginga" last="Shimakawa">Ginga Shimakawa</name></region><name sortKey="Miyake, Chikahiro" 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