H-2-driven biotransformation of n-octane to 1-octanol by a recombinant Pseudomonas putida strain co-synthesizing an O-2-tolerant hydrogenase and a P450 monooxygenase

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dc.contributor.authorLonsdale, Thomas H.
dc.contributor.authorLauterbach, Lars
dc.contributor.authorMalca, Sumire Honda
dc.contributor.authorNestl, Bettina M.
dc.contributor.authorHauer, Bernhard
dc.contributor.authorLenz, Oliver
dc.date.accessioned2017-10-25T06:24:48Z
dc.date.available2017-10-25T06:24:48Z
dc.date.issued2015
dc.description.abstractAn in vivo biotransformation system is presented that affords the hydroxylation of n-octane to 1-octanol on the basis of NADH-dependent CYP153A monooxygenase and NAD(+)-reducing hydrogenase heterologously synthesized in a bacterial host. The hydrogenase sustains H-2-driven NADH cofactor regeneration even in the presence of O-2, the co-substrate of monooxygenase.en
dc.description.sponsorshipDFG, EXC 314, Unifying Concepts in Catalysisen
dc.description.sponsorshipEC/FP7/297503/EU/Modular beads for regeneration of bio-cofactors in enzyme-catalysed synthesis/HydRegenen
dc.identifier.eissn1364-548X
dc.identifier.issn1359-7345
dc.identifier.pmid26394141
dc.identifier.urihttps://depositonce.tu-berlin.de/handle/11303/6933
dc.identifier.urihttp://dx.doi.org/10.14279/depositonce-6272
dc.language.isoen
dc.rights.urihttps://creativecommons.org/licenses/by/3.0/
dc.subject.ddc540 Chemie und zugeordnete Wissenschaftende
dc.titleH-2-driven biotransformation of n-octane to 1-octanol by a recombinant Pseudomonas putida strain co-synthesizing an O-2-tolerant hydrogenase and a P450 monooxygenaseen
dc.typeArticleen
dc.type.versionpublishedVersionen
dcterms.bibliographicCitation.doi10.1039/c5cc06078h
dcterms.bibliographicCitation.issue90
dcterms.bibliographicCitation.journaltitleChemical communicationsen
dcterms.bibliographicCitation.originalpublishernameRoyal Society of Chemistryde
dcterms.bibliographicCitation.originalpublisherplaceCambridgede
dcterms.bibliographicCitation.pageend16175
dcterms.bibliographicCitation.pagestart16173
dcterms.bibliographicCitation.volume51
tub.accessrights.dnbfree
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 Berlin

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