Dihydrogen-driven NADPH recycling in imine reduction and P450-catalyzed oxidations mediated by an engineered O2-tolerant hydrogenase

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dc.contributor.authorPreissler, Janina
dc.contributor.authorReeve, Holly A.
dc.contributor.authorZhu, Tianze
dc.contributor.authorNicholson, Jake
dc.contributor.authorUrata, Kouji
dc.contributor.authorLauterbach, Lars
dc.contributor.authorWong, Luet L.
dc.contributor.authorVincent, Kylie A.
dc.contributor.authorLenz, Oliver
dc.date.accessioned2021-06-10T06:56:57Z
dc.date.available2021-06-10T06:56:57Z
dc.date.issued2020-06-16
dc.description.abstractThe O2-tolerant NAD+-reducing hydrogenase (SH) from Ralstonia eutropha (Cupriavidus necator) has already been applied in vitro and in vivo for H2-driven NADH recycling in coupled enzymatic reactions with various NADH-dependent oxidoreductases. To expand the scope for application in NADPH-dependent biocatalysis, we introduced changes in the NAD+-binding pocket of the enzyme by rational mutagenesis, and generated a variant with significantly higher affinity for NADP+ than for the natural substrate NAD+, while retaining native O2-tolerance. The applicability of the SH variant in H2-driven NADPH supply was demonstrated by the full conversion of 2-methyl-1-pyrroline into a single enantiomer of 2-methylpyrrolidine catalysed by a stereoselective imine reductase. In an even more challenging reaction, the SH supported a cytochrome P450 monooxygenase for the oxidation of octane under safe H2/O2 mixtures. Thus, the re-designed SH represents a versatile platform for atom-efficient, H2-driven cofactor recycling in biotransformations involving NADPH-dependent oxidoreductases.en
dc.description.sponsorshipDFG, 390540038, EXC 2008: Unifying Systems in Catalysis "UniSysCat"en
dc.description.sponsorshipTU Berlin, Open-Access-Mittel – 2020en
dc.identifier.eissn1867-3899
dc.identifier.issn1867-3880
dc.identifier.urihttps://depositonce.tu-berlin.de/handle/11303/13228
dc.identifier.urihttp://dx.doi.org/10.14279/depositonce-12023
dc.language.isoenen
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/en
dc.subject.ddc540 Chemie und zugeordnete Wissenschaftende
dc.subject.otherhydrogenaseen
dc.subject.othermetalloenzymeen
dc.subject.othercytochrome P450en
dc.subject.othermonooxygenaseen
dc.subject.otheroxidoreductaseen
dc.subject.otherimine reductaseen
dc.subject.otheroctane oxidationen
dc.subject.othernicotinamide cofactoren
dc.subject.otherNADHen
dc.subject.othercofactor recyclingen
dc.titleDihydrogen-driven NADPH recycling in imine reduction and P450-catalyzed oxidations mediated by an engineered O2-tolerant hydrogenaseen
dc.typeArticleen
dc.type.versionpublishedVersionen
dcterms.bibliographicCitation.doi10.1002/cctc.202000763en
dcterms.bibliographicCitation.issue19en
dcterms.bibliographicCitation.journaltitleChemCatChemen
dcterms.bibliographicCitation.originalpublishernameWileyen
dcterms.bibliographicCitation.originalpublisherplaceNew York, NYen
dcterms.bibliographicCitation.pageend4861en
dcterms.bibliographicCitation.pagestart4853en
dcterms.bibliographicCitation.volume12en
tub.accessrights.dnbfreeen
tub.affiliationFak. 2 Mathematik und Naturwissenschaften::Inst. Chemie::FG Physikalische Chemie / Biophysikalische Chemiede
tub.affiliation.facultyFak. 2 Mathematik und Naturwissenschaftende
tub.affiliation.groupFG Physikalische Chemie / Biophysikalische Chemiede
tub.affiliation.instituteInst. Chemiede
tub.publisher.universityorinstitutionTechnische Universität Berlinen

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