Please use this identifier to cite or link to this item: http://dx.doi.org/10.14279/depositonce-6272
Main Title: 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
Author(s): Lonsdale, Thomas H.
Lauterbach, Lars
Malca, Sumire Honda
Nestl, Bettina M.
Hauer, Bernhard
Lenz, Oliver
Type: Article
Language Code: en
Abstract: An 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.
URI: https://depositonce.tu-berlin.de//handle/11303/6933
http://dx.doi.org/10.14279/depositonce-6272
Issue Date: 2015
Date Available: 25-Oct-2017
DDC Class: 540 Chemie und zugeordnete Wissenschaften
Sponsor/Funder: DFG, EXC 314, Unifying Concepts in Catalysis
EC/FP7/297503/EU/Modular beads for regeneration of bio-cofactors in enzyme-catalysed synthesis/HydRegen
Creative Commons License: https://creativecommons.org/licenses/by/3.0/
Journal Title: Chemical communications
Publisher: Royal Society of Chemistry
Publisher Place: Cambridge
Volume: 51
Issue: 90
Publisher DOI: 10.1039/c5cc06078h
Page Start: 16173
Page End: 16175
EISSN: 1364-548X
ISSN: 1359-7345
Appears in Collections:Fachgebiet Physikalische Chemie / Biophysikalische Chemie » Publications

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