CO synthesized from the central one-carbon pool as source for the iron carbonyl in O2-tolerant [NiFe]-hydrogenase
Identifieur interne : 000762 ( Ncbi/Merge ); précédent : 000761; suivant : 000763CO synthesized from the central one-carbon pool as source for the iron carbonyl in O2-tolerant [NiFe]-hydrogenase
Auteurs : Ingmar Bürstel [Allemagne] ; Elisabeth Siebert [Allemagne] ; Stefan Frielingsdorf [Allemagne] ; Ingo Zebger [Allemagne] ; B Rbel Friedrich [Allemagne] ; Oliver Lenz [Allemagne]Source :
- Proceedings of the National Academy of Sciences of the United States of America [ 0027-8424 ] ; 2016.
Abstract
Activation of dihydrogen is by far not a trivial catalytic reaction. Microbes have evolved sophisticated hydrogenases with complex transition metal centers to get access to H2. A recurring feature of these centers is the presence of iron atoms equipped with carbon monoxide ligands. In case of [NiFe]-hydrogenases, which contain a NiFe(CN)2CO catalytic center, biosynthesis of the toxic CO ligand remained elusive. We show that [NiFe]-hydrogenases that are catalytically active in the presence of dioxygen use a dedicated maturase for CO ligand synthesis under aerobic conditions. CO is derived from the most oxidized intermediate of the central one-carbon metabolism, formyl-tetrahydrofolate. This discovery contributes a so far unknown reaction to the one-carbon metabolism and opens perspectives for chemical and of bioinspired catalysis.
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DOI: 10.1073/pnas.1614656113
PubMed: 27930319
PubMed Central: 5187695
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carbonyl in O<sub>2</sub>-tolerant [NiFe]-hydrogenase</title><author><name sortKey="Burstel, Ingmar" sort="Burstel, Ingmar" uniqKey="Burstel I" first="Ingmar" last="Bürstel">Ingmar Bürstel</name><affiliation wicri:level="1"><nlm:aff id="aff1">Department of Biology, Microbiology,<institution>Humboldt-Universität zu Berlin</institution>, 10115 Berlin,<country>Germany</country>;</nlm:aff><country xml:lang="fr">Allemagne</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation><affiliation wicri:level="1"><nlm:aff id="aff2">Department of Chemistry, Biophysical Chemistry,<institution>Technische Universität Berlin</institution>, 10623 Berlin,<country>Germany</country></nlm:aff><country xml:lang="fr">Allemagne</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation></author><author><name sortKey="Siebert, Elisabeth" sort="Siebert, Elisabeth" uniqKey="Siebert E" first="Elisabeth" last="Siebert">Elisabeth Siebert</name><affiliation wicri:level="1"><nlm:aff id="aff2">Department of Chemistry, Biophysical Chemistry,<institution>Technische Universität Berlin</institution>, 10623 Berlin,<country>Germany</country></nlm:aff><country xml:lang="fr">Allemagne</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation></author><author><name sortKey="Frielingsdorf, Stefan" sort="Frielingsdorf, Stefan" uniqKey="Frielingsdorf S" first="Stefan" last="Frielingsdorf">Stefan Frielingsdorf</name><affiliation wicri:level="1"><nlm:aff id="aff1">Department of Biology, Microbiology,<institution>Humboldt-Universität zu Berlin</institution>, 10115 Berlin,<country>Germany</country>;</nlm:aff><country xml:lang="fr">Allemagne</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation><affiliation wicri:level="1"><nlm:aff id="aff2">Department of Chemistry, Biophysical Chemistry,<institution>Technische Universität Berlin</institution>, 10623 Berlin,<country>Germany</country></nlm:aff><country xml:lang="fr">Allemagne</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation></author><author><name sortKey="Zebger, Ingo" sort="Zebger, Ingo" uniqKey="Zebger I" first="Ingo" last="Zebger">Ingo Zebger</name><affiliation wicri:level="1"><nlm:aff id="aff2">Department of Chemistry, Biophysical Chemistry,<institution>Technische Universität Berlin</institution>, 10623 Berlin,<country>Germany</country></nlm:aff><country xml:lang="fr">Allemagne</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation></author><author><name sortKey="Friedrich, B Rbel" sort="Friedrich, B Rbel" uniqKey="Friedrich B" first="B Rbel" last="Friedrich">B Rbel Friedrich</name><affiliation wicri:level="1"><nlm:aff id="aff1">Department of Biology, Microbiology,<institution>Humboldt-Universität zu Berlin</institution>, 10115 Berlin,<country>Germany</country>;</nlm:aff><country xml:lang="fr">Allemagne</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation></author><author><name sortKey="Lenz, Oliver" sort="Lenz, Oliver" uniqKey="Lenz O" first="Oliver" last="Lenz">Oliver Lenz</name><affiliation wicri:level="1"><nlm:aff id="aff1">Department of Biology, Microbiology,<institution>Humboldt-Universität zu Berlin</institution>, 10115 Berlin,<country>Germany</country>;</nlm:aff><country xml:lang="fr">Allemagne</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation><affiliation wicri:level="1"><nlm:aff id="aff2">Department of Chemistry, Biophysical Chemistry,<institution>Technische Universität Berlin</institution>, 10623 Berlin,<country>Germany</country></nlm:aff><country xml:lang="fr">Allemagne</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation></author></analytic><series><title level="j">Proceedings of the National Academy of Sciences of the United States of America</title><idno type="ISSN">0027-8424</idno><idno type="eISSN">1091-6490</idno><imprint><date when="2016">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><title>Significance</title><p>Activation of dihydrogen is by far not a trivial catalytic reaction. Microbes have evolved sophisticated hydrogenases with complex transition metal centers to get access to H<sub>2</sub>. A recurring feature of these centers is the presence of iron atoms equipped with carbon monoxide ligands. In case of [NiFe]-hydrogenases, which contain a NiFe(CN)<sub>2</sub>CO catalytic center, biosynthesis of the toxic CO ligand remained elusive. We show that [NiFe]-hydrogenases that are catalytically active in the presence of dioxygen use a dedicated maturase for CO ligand synthesis under aerobic conditions. CO is derived from the most oxidized intermediate of the central one-carbon metabolism, formyl-tetrahydrofolate. This discovery contributes a so far unknown reaction to the one-carbon metabolism and opens perspectives for chemical and of bioinspired catalysis.</p></div></front></TEI><pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Proc Natl Acad Sci U S A</journal-id><journal-id journal-id-type="iso-abbrev">Proc. Natl. Acad. Sci. U.S.A</journal-id><journal-id journal-id-type="hwp">pnas</journal-id><journal-id journal-id-type="pmc">pnas</journal-id><journal-id journal-id-type="publisher-id">PNAS</journal-id><journal-title-group><journal-title>Proceedings of the National Academy of Sciences of the United States of America</journal-title></journal-title-group><issn pub-type="ppub">0027-8424</issn><issn pub-type="epub">1091-6490</issn><publisher><publisher-name>National Academy of Sciences</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">27930319</article-id><article-id pub-id-type="pmc">5187695</article-id><article-id pub-id-type="publisher-id">201614656</article-id><article-id pub-id-type="doi">10.1073/pnas.1614656113</article-id><article-categories><subj-group subj-group-type="heading"><subject>Biological Sciences</subject><subj-group><subject>Biochemistry</subject></subj-group></subj-group></article-categories><title-group><article-title>CO synthesized from the central one-carbon pool as source for the iron carbonyl in O<sub>2</sub>-tolerant [NiFe]-hydrogenase</article-title><alt-title alt-title-type="short">Carbonyl ligand synthesis of [NiFe]-hydrogenase</alt-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Bürstel</surname><given-names>Ingmar</given-names></name><xref ref-type="aff" rid="aff1"><sup>a</sup></xref><xref ref-type="aff" rid="aff2"><sup>b</sup></xref></contrib><contrib contrib-type="author"><name><surname>Siebert</surname><given-names>Elisabeth</given-names></name><xref ref-type="aff" rid="aff2"><sup>b</sup></xref></contrib><contrib contrib-type="author"><contrib-id contrib-id-type="orcid" authenticated="false">http://orcid.org/0000-0002-4141-7836</contrib-id><name><surname>Frielingsdorf</surname><given-names>Stefan</given-names></name><xref ref-type="aff" rid="aff1"><sup>a</sup></xref><xref ref-type="aff" rid="aff2"><sup>b</sup></xref></contrib><contrib contrib-type="author"><name><surname>Zebger</surname><given-names>Ingo</given-names></name><xref ref-type="aff" rid="aff2"><sup>b</sup></xref></contrib><contrib contrib-type="author"><name><surname>Friedrich</surname><given-names>Bärbel</given-names></name><xref ref-type="aff" rid="aff1"><sup>a</sup></xref></contrib><contrib contrib-type="author"><contrib-id contrib-id-type="orcid" authenticated="false">http://orcid.org/0000-0003-4550-5128</contrib-id><name><surname>Lenz</surname><given-names>Oliver</given-names></name><xref ref-type="aff" rid="aff1"><sup>a</sup></xref><xref ref-type="aff" rid="aff2"><sup>b</sup></xref><xref ref-type="corresp" rid="cor1"><sup>1</sup></xref></contrib><aff id="aff1"><sup>a</sup>Department of Biology, Microbiology,<institution>Humboldt-Universität zu Berlin</institution>, 10115 Berlin,<country>Germany</country>;</aff><aff id="aff2"><sup>b</sup>Department of Chemistry, Biophysical Chemistry,<institution>Technische Universität Berlin</institution>, 10623 Berlin,<country>Germany</country></aff></contrib-group><author-notes><corresp id="cor1"><sup>1</sup>To whom correspondence should be addressed. Email: <email>oliver.lenz@tu-berlin.de</email>.</corresp><fn fn-type="edited-by"><p>Edited by Harry B. Gray, California Institute of Technology, Pasadena, CA, and approved November 8, 2016 (received for review September 1, 2016)</p></fn><fn fn-type="con"><p>Author contributions: I.B. and O.L. designed research; I.B., E.S., S.F., and I.Z. performed research; I.B., E.S., S.F., and O.L. analyzed data; and I.B., I.Z., B.F., and O.L. wrote the paper.</p></fn><fn fn-type="COI-statement"><p>The authors declare no conflict of interest.</p></fn></author-notes><pub-date pub-type="ppub"><day>20</day><month>12</month><year>2016</year></pub-date><pub-date pub-type="epub"><day>5</day><month>12</month><year>2016</year></pub-date><volume>113</volume><issue>51</issue><fpage>14722</fpage><lpage>14726</lpage><permissions></permissions><self-uri xlink:title="pdf" xlink:href="pnas.201614656.pdf"></self-uri><abstract abstract-type="executive-summary"><title>Significance</title><p>Activation of dihydrogen is by far not a trivial catalytic reaction. Microbes have evolved sophisticated hydrogenases with complex transition metal centers to get access to H<sub>2</sub>. A recurring feature of these centers is the presence of iron atoms equipped with carbon monoxide ligands. In case of [NiFe]-hydrogenases, which contain a NiFe(CN)<sub>2</sub>CO catalytic center, biosynthesis of the toxic CO ligand remained elusive. We show that [NiFe]-hydrogenases that are catalytically active in the presence of dioxygen use a dedicated maturase for CO ligand synthesis under aerobic conditions. CO is derived from the most oxidized intermediate of the central one-carbon metabolism, formyl-tetrahydrofolate. This discovery contributes a so far unknown reaction to the one-carbon metabolism and opens perspectives for chemical and of bioinspired catalysis.</p></abstract><abstract><p>Hydrogenases are nature’s key catalysts involved in both microbial consumption and production of molecular hydrogen. H<sub>2</sub> exhibits a strongly bonded, almost inert electron pair and requires transition metals for activation. Consequently, all hydrogenases are metalloenzymes that contain at least one iron atom in the catalytic center. For appropriate interaction with H<sub>2</sub>, the iron moiety demands for a sophisticated coordination environment that cannot be provided just by standard amino acids. This dilemma has been overcome by the introduction of unprecedented chemistry—that is, by ligating the iron with carbon monoxide (CO) and cyanide (or equivalent) groups. These ligands are both unprecedented in microbial metabolism and, in their free form, highly toxic to living organisms. Therefore, the formation of the diatomic ligands relies on dedicated biosynthesis pathways. So far, biosynthesis of the CO ligand in [NiFe]-hydrogenases was unknown. Here we show that the aerobic H<sub>2</sub> oxidizer <italic>Ralstonia eutropha</italic>, which produces active [NiFe]-hydrogenases in the presence of O<sub>2</sub>, employs the auxiliary protein HypX (hydrogenase pleiotropic maturation X) for CO ligand formation. Using genetic engineering and isotope labeling experiments in combination with infrared spectroscopic investigations, we demonstrate that the α-carbon of glycine ends up in the CO ligand of [NiFe]-hydrogenase. The α-carbon of glycine is a building block of the central one-carbon metabolism intermediate, <italic>N</italic><sup>10</sup>-formyl-tetrahydrofolate (<italic>N</italic><sup>10</sup>-CHO-THF). Evidence is presented that the multidomain protein, HypX, converts the formyl group of <italic>N</italic><sup>10</sup>-CHO-THF into water and CO, thereby providing the carbonyl ligand for hydrogenase. This study contributes insights into microbial biosynthesis of metal carbonyls involving toxic intermediates.</p></abstract><kwd-group><kwd>hydrogenase</kwd><kwd>metalloenzyme</kwd><kwd>carbonyl ligand</kwd><kwd>formyl-THF</kwd><kwd>one-carbon metabolism</kwd></kwd-group><funding-group><award-group id="gs1"><funding-source id="sp1">Deutsche Forschungsgemeinschaft (DFG)<named-content content-type="funder-id">501100001659</named-content></funding-source><award-id rid="sp1">EXC 314</award-id></award-group><award-group id="gs2"><funding-source id="sp2">Deutsche Forschungsgemeinschaft (DFG)<named-content content-type="funder-id">501100001659</named-content></funding-source><award-id rid="sp2">SPP 1927</award-id></award-group></funding-group><counts><page-count count="5"></page-count></counts></article-meta></front></pmc><affiliations><list><country><li>Allemagne</li></country></list><tree><country name="Allemagne"><noRegion><name sortKey="Burstel, Ingmar" sort="Burstel, Ingmar" uniqKey="Burstel I" first="Ingmar" last="Bürstel">Ingmar Bürstel</name></noRegion><name sortKey="Burstel, Ingmar" sort="Burstel, Ingmar" uniqKey="Burstel I" first="Ingmar" last="Bürstel">Ingmar Bürstel</name><name sortKey="Friedrich, B Rbel" sort="Friedrich, B Rbel" uniqKey="Friedrich B" first="B Rbel" last="Friedrich">B Rbel Friedrich</name><name sortKey="Frielingsdorf, Stefan" sort="Frielingsdorf, Stefan" uniqKey="Frielingsdorf S" first="Stefan" last="Frielingsdorf">Stefan Frielingsdorf</name><name sortKey="Frielingsdorf, Stefan" sort="Frielingsdorf, Stefan" uniqKey="Frielingsdorf S" first="Stefan" last="Frielingsdorf">Stefan Frielingsdorf</name><name sortKey="Lenz, Oliver" sort="Lenz, Oliver" uniqKey="Lenz O" first="Oliver" last="Lenz">Oliver Lenz</name><name sortKey="Lenz, Oliver" sort="Lenz, Oliver" uniqKey="Lenz O" first="Oliver" last="Lenz">Oliver Lenz</name><name sortKey="Siebert, Elisabeth" sort="Siebert, Elisabeth" uniqKey="Siebert E" first="Elisabeth" last="Siebert">Elisabeth Siebert</name><name sortKey="Zebger, Ingo" sort="Zebger, Ingo" uniqKey="Zebger I" first="Ingo" last="Zebger">Ingo Zebger</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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