The structure and reactivity of the HoxEFU complex from the cyanobacterium Synechocystis sp. PCC 6803.
Identifieur interne : 000011 ( Main/Exploration ); précédent : 000010; suivant : 000012The structure and reactivity of the HoxEFU complex from the cyanobacterium Synechocystis sp. PCC 6803.
Auteurs : Jacob H. Artz [États-Unis] ; Monika Tokmina-Lukaszewska [États-Unis] ; David W. Mulder [États-Unis] ; Carolyn E. Lubner [États-Unis] ; Kirstin Gutekunst [Allemagne] ; Jens Appel [Allemagne] ; Brian Bothner [États-Unis] ; Marko Boehm [Allemagne] ; Paul W. KingSource :
- The Journal of biological chemistry [ 1083-351X ] ; 2020.
Abstract
Cyanobacterial Hox is a [NiFe] hydrogenase that consists of the hydrogen (H2)-activating subunits HoxYH, which form a complex with the HoxEFU assembly to mediate reactions with soluble electron carriers like NAD(P)H and ferredoxin (Fdx), thereby coupling photosynthetic electron transfer to energy-transforming catalytic reactions. Researchers studying the HoxEFUYH complex have observed that HoxEFU can be isolated independently of HoxYH, leading to the hypothesis that HoxEFU is a distinct functional subcomplex rather than an artifact of Hox complex isolation. Moreover, outstanding questions about the reactivity of Hox with natural substrates and the site(s) of substrate interactions and coupling of H2, NAD(P)H, and Fdx remain to be resolved. To address these questions, here we analyzed recombinantly produced HoxEFU by electron paramagnetic resonance spectroscopy and kinetic assays with natural substrates. The purified HoxEFU subcomplex catalyzed electron transfer reactions among NAD(P)H, flavodoxin, and several ferredoxins, thus functioning in vitro as a shuttle among different cyanobacterial pools of reducing equivalents. Both Fdx1-dependent reductions of NAD+ and NADP+ were cooperative. HoxEFU also catalyzed the flavodoxin-dependent reduction of NAD(P)+, Fdx2-dependent oxidation of NADH and Fdx4- and Fdx11-dependent reduction of NAD+ MS-based mapping identified an Fdx1-binding site at the junction of HoxE and HoxF, adjacent to iron-sulfur (FeS) clusters in both subunits. Overall, the reactivity of HoxEFU observed here suggests that it functions in managing peripheral electron flow from photosynthetic electron transfer, findings that reveal detailed insights into how ubiquitous cellular components may be used to allocate energy flow into specific bioenergetic products.
DOI: 10.1074/jbc.RA120.013136
PubMed: 32409585
PubMed Central: PMC7363133
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PCC 6803.</title><author><name sortKey="Artz, Jacob H" sort="Artz, Jacob H" uniqKey="Artz J" first="Jacob H" last="Artz">Jacob H. Artz</name><affiliation wicri:level="2"><nlm:affiliation>Biosciences Center, National Renewable Energy Laboratory, Golden, Colorado, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Biosciences Center, National Renewable Energy Laboratory, Golden, Colorado</wicri:regionArea><placeName><region type="state">Colorado</region></placeName></affiliation></author><author><name sortKey="Tokmina Lukaszewska, Monika" sort="Tokmina Lukaszewska, Monika" uniqKey="Tokmina Lukaszewska M" first="Monika" last="Tokmina-Lukaszewska">Monika Tokmina-Lukaszewska</name><affiliation wicri:level="2"><nlm:affiliation>Department of Chemistry and Biochemistry, Montana State University, Bozeman, Montana, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Chemistry and Biochemistry, Montana State University, Bozeman, Montana</wicri:regionArea><placeName><region type="state">Montana</region></placeName></affiliation></author><author><name sortKey="Mulder, David W" sort="Mulder, David W" uniqKey="Mulder D" first="David W" last="Mulder">David W. Mulder</name><affiliation wicri:level="2"><nlm:affiliation>Biosciences Center, National Renewable Energy Laboratory, Golden, Colorado, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Biosciences Center, National Renewable Energy Laboratory, Golden, Colorado</wicri:regionArea><placeName><region type="state">Colorado</region></placeName></affiliation></author><author><name sortKey="Lubner, Carolyn E" sort="Lubner, Carolyn E" uniqKey="Lubner C" first="Carolyn E" last="Lubner">Carolyn E. Lubner</name><affiliation wicri:level="2"><nlm:affiliation>Biosciences Center, National Renewable Energy Laboratory, Golden, Colorado, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Biosciences Center, National Renewable Energy Laboratory, Golden, Colorado</wicri:regionArea><placeName><region type="state">Colorado</region></placeName></affiliation></author><author><name sortKey="Gutekunst, Kirstin" sort="Gutekunst, Kirstin" uniqKey="Gutekunst K" first="Kirstin" last="Gutekunst">Kirstin Gutekunst</name><affiliation wicri:level="3"><nlm:affiliation>Botanical Institute, Christian-Albrechts-University, Kiel, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Botanical Institute, Christian-Albrechts-University, Kiel</wicri:regionArea><placeName><region type="land" nuts="2">Schleswig-Holstein</region><settlement type="city">Kiel</settlement></placeName></affiliation></author><author><name sortKey="Appel, Jens" sort="Appel, Jens" uniqKey="Appel J" first="Jens" last="Appel">Jens Appel</name><affiliation wicri:level="3"><nlm:affiliation>Botanical Institute, Christian-Albrechts-University, Kiel, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Botanical Institute, Christian-Albrechts-University, Kiel</wicri:regionArea><placeName><region type="land" nuts="2">Schleswig-Holstein</region><settlement type="city">Kiel</settlement></placeName></affiliation></author><author><name sortKey="Bothner, Brian" sort="Bothner, Brian" uniqKey="Bothner B" first="Brian" last="Bothner">Brian Bothner</name><affiliation wicri:level="2"><nlm:affiliation>Department of Chemistry and Biochemistry, Montana State University, Bozeman, Montana, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Chemistry and Biochemistry, Montana State University, Bozeman, Montana</wicri:regionArea><placeName><region type="state">Montana</region></placeName></affiliation></author><author><name sortKey="Boehm, Marko" sort="Boehm, Marko" uniqKey="Boehm M" first="Marko" last="Boehm">Marko Boehm</name><affiliation wicri:level="3"><nlm:affiliation>Botanical Institute, Christian-Albrechts-University, Kiel, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Botanical Institute, Christian-Albrechts-University, Kiel</wicri:regionArea><placeName><region type="land" nuts="2">Schleswig-Holstein</region><settlement type="city">Kiel</settlement></placeName></affiliation></author><author><name sortKey="King, Paul W" sort="King, Paul W" uniqKey="King P" first="Paul W" last="King">Paul W. King</name><affiliation><nlm:affiliation>Biosciences Center, National Renewable Energy Laboratory, Golden, Colorado, USA paul.king@nrel.gov.</nlm:affiliation><wicri:noCountry code="subField">USA paul.king@nrel.gov.</wicri:noCountry></affiliation></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="eISSN">1083-351X</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Cyanobacterial Hox is a [NiFe] hydrogenase that consists of the hydrogen (H<sub>2</sub>)-activating subunits HoxYH, which form a complex with the HoxEFU assembly to mediate reactions with soluble electron carriers like NAD(P)H and ferredoxin (Fdx), thereby coupling photosynthetic electron transfer to energy-transforming catalytic reactions. Researchers studying the HoxEFUYH complex have observed that HoxEFU can be isolated independently of HoxYH, leading to the hypothesis that HoxEFU is a distinct functional subcomplex rather than an artifact of Hox complex isolation. Moreover, outstanding questions about the reactivity of Hox with natural substrates and the site(s) of substrate interactions and coupling of H<sub>2</sub>, NAD(P)H, and Fdx remain to be resolved. To address these questions, here we analyzed recombinantly produced HoxEFU by electron paramagnetic resonance spectroscopy and kinetic assays with natural substrates. The purified HoxEFU subcomplex catalyzed electron transfer reactions among NAD(P)H, flavodoxin, and several ferredoxins, thus functioning <i>in vitro</i> as a shuttle among different cyanobacterial pools of reducing equivalents. Both Fdx1-dependent reductions of NAD<sup>+</sup> and NADP<sup>+</sup> were cooperative. HoxEFU also catalyzed the flavodoxin-dependent reduction of NAD(P)<sup>+</sup>, Fdx2-dependent oxidation of NADH and Fdx4- and Fdx11-dependent reduction of NAD<sup>+</sup> MS-based mapping identified an Fdx1-binding site at the junction of HoxE and HoxF, adjacent to iron-sulfur (FeS) clusters in both subunits. Overall, the reactivity of HoxEFU observed here suggests that it functions in managing peripheral electron flow from photosynthetic electron transfer, findings that reveal detailed insights into how ubiquitous cellular components may be used to allocate energy flow into specific bioenergetic products.</div></front></TEI><pubmed><MedlineCitation Status="In-Data-Review" Owner="NLM"><PMID Version="1">32409585</PMID><DateRevised><Year>2020</Year><Month>07</Month><Day>25</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1083-351X</ISSN><JournalIssue CitedMedium="Internet"><Volume>295</Volume><Issue>28</Issue><PubDate><Year>2020</Year><Month>Jul</Month><Day>10</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>The structure and reactivity of the HoxEFU complex from the cyanobacterium <i>Synechocystis</i> sp. PCC 6803.</ArticleTitle><Pagination><MedlinePgn>9445-9454</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1074/jbc.RA120.013136</ELocationID><Abstract><AbstractText>Cyanobacterial Hox is a [NiFe] hydrogenase that consists of the hydrogen (H<sub>2</sub>)-activating subunits HoxYH, which form a complex with the HoxEFU assembly to mediate reactions with soluble electron carriers like NAD(P)H and ferredoxin (Fdx), thereby coupling photosynthetic electron transfer to energy-transforming catalytic reactions. Researchers studying the HoxEFUYH complex have observed that HoxEFU can be isolated independently of HoxYH, leading to the hypothesis that HoxEFU is a distinct functional subcomplex rather than an artifact of Hox complex isolation. Moreover, outstanding questions about the reactivity of Hox with natural substrates and the site(s) of substrate interactions and coupling of H<sub>2</sub>, NAD(P)H, and Fdx remain to be resolved. To address these questions, here we analyzed recombinantly produced HoxEFU by electron paramagnetic resonance spectroscopy and kinetic assays with natural substrates. The purified HoxEFU subcomplex catalyzed electron transfer reactions among NAD(P)H, flavodoxin, and several ferredoxins, thus functioning <i>in vitro</i> as a shuttle among different cyanobacterial pools of reducing equivalents. Both Fdx1-dependent reductions of NAD<sup>+</sup> and NADP<sup>+</sup> were cooperative. HoxEFU also catalyzed the flavodoxin-dependent reduction of NAD(P)<sup>+</sup>, Fdx2-dependent oxidation of NADH and Fdx4- and Fdx11-dependent reduction of NAD<sup>+</sup> MS-based mapping identified an Fdx1-binding site at the junction of HoxE and HoxF, adjacent to iron-sulfur (FeS) clusters in both subunits. Overall, the reactivity of HoxEFU observed here suggests that it functions in managing peripheral electron flow from photosynthetic electron transfer, findings that reveal detailed insights into how ubiquitous cellular components may be used to allocate energy flow into specific bioenergetic products.</AbstractText><CopyrightInformation>© 2020 Artz et al.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Artz</LastName><ForeName>Jacob H</ForeName><Initials>JH</Initials><AffiliationInfo><Affiliation>Biosciences Center, National Renewable Energy Laboratory, Golden, Colorado, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Tokmina-Lukaszewska</LastName><ForeName>Monika</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Department of Chemistry and Biochemistry, Montana State University, Bozeman, Montana, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mulder</LastName><ForeName>David W</ForeName><Initials>DW</Initials><AffiliationInfo><Affiliation>Biosciences Center, National Renewable Energy Laboratory, Golden, Colorado, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lubner</LastName><ForeName>Carolyn E</ForeName><Initials>CE</Initials><AffiliationInfo><Affiliation>Biosciences Center, National Renewable Energy Laboratory, Golden, Colorado, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gutekunst</LastName><ForeName>Kirstin</ForeName><Initials>K</Initials><Identifier Source="ORCID">https://orcid.org/0000-0003-4366-423X</Identifier><AffiliationInfo><Affiliation>Botanical Institute, Christian-Albrechts-University, Kiel, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Appel</LastName><ForeName>Jens</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Botanical Institute, Christian-Albrechts-University, Kiel, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bothner</LastName><ForeName>Brian</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Department of Chemistry and Biochemistry, Montana State University, Bozeman, Montana, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Boehm</LastName><ForeName>Marko</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Botanical Institute, Christian-Albrechts-University, Kiel, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>King</LastName><ForeName>Paul W</ForeName><Initials>PW</Initials><Identifier Source="ORCID">https://orcid.org/0000-0001-5039-654X</Identifier><AffiliationInfo><Affiliation>Biosciences Center, National Renewable Energy Laboratory, Golden, Colorado, USA paul.king@nrel.gov.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>P20 GM103474</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2020</Year><Month>05</Month><Day>14</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><CitationSubset>IM</CitationSubset><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">HoxEFU</Keyword><Keyword MajorTopicYN="N">Synechocystis</Keyword><Keyword MajorTopicYN="N">bidirectional hydrogenase</Keyword><Keyword MajorTopicYN="N">cooperativity</Keyword><Keyword MajorTopicYN="N">diaphorase</Keyword><Keyword MajorTopicYN="N">electron paramagnetic resonance (EPR)</Keyword><Keyword MajorTopicYN="N">hydrogenase</Keyword><Keyword MajorTopicYN="N">kinetics</Keyword><Keyword MajorTopicYN="N">nickel</Keyword><Keyword MajorTopicYN="N">nickel-iron enzyme</Keyword><Keyword MajorTopicYN="N">photosynthesis</Keyword><Keyword MajorTopicYN="N">protein cross-linking</Keyword><Keyword MajorTopicYN="N">protein-protein interaction</Keyword></KeywordList><CoiStatement>Conflict of interest—The authors declare that they have no conflicts of interest with the contents of this article.</CoiStatement></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2020</Year><Month>02</Month><Day>19</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2020</Year><Month>05</Month><Day>11</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>5</Month><Day>16</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>5</Month><Day>16</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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King</name></noCountry><country name="États-Unis"><region name="Colorado"><name sortKey="Artz, Jacob H" sort="Artz, Jacob H" uniqKey="Artz J" first="Jacob H" last="Artz">Jacob H. Artz</name></region><name sortKey="Bothner, Brian" sort="Bothner, Brian" uniqKey="Bothner B" first="Brian" last="Bothner">Brian Bothner</name><name sortKey="Lubner, Carolyn E" sort="Lubner, Carolyn E" uniqKey="Lubner C" first="Carolyn E" last="Lubner">Carolyn E. Lubner</name><name sortKey="Mulder, David W" sort="Mulder, David W" uniqKey="Mulder D" first="David W" last="Mulder">David W. Mulder</name><name sortKey="Tokmina Lukaszewska, Monika" sort="Tokmina Lukaszewska, Monika" uniqKey="Tokmina Lukaszewska M" first="Monika" last="Tokmina-Lukaszewska">Monika Tokmina-Lukaszewska</name></country><country name="Allemagne"><region name="Schleswig-Holstein"><name sortKey="Gutekunst, Kirstin" sort="Gutekunst, Kirstin" uniqKey="Gutekunst K" first="Kirstin" last="Gutekunst">Kirstin Gutekunst</name></region><name sortKey="Appel, Jens" sort="Appel, Jens" uniqKey="Appel J" first="Jens" last="Appel">Jens Appel</name><name sortKey="Boehm, Marko" sort="Boehm, Marko" uniqKey="Boehm M" first="Marko" last="Boehm">Marko Boehm</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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