Issue 90, 2015
From the journal:

Chemical Communications

H2-driven biotransformation of n-octane to 1-octanol by a recombinant Pseudomonas putida strain co-synthesizing an O2-tolerant hydrogenase and a P450 monooxygenase†

Thomas H. Lonsdale,‡ab   Lars Lauterbach,‡*a   Sumire Honda Malca,c   Bettina M. Nestl,c   Bernhard Hauerc  and  Oliver Lenz*a  

* Corresponding authors

a Department of Chemistry, Technische Universität Berlin, Straße des 17. Juni 135, 10623 Berlin, Germany
E-mail: lars.lauterbach@tu-berlin.de, oliver.lenz@tu-berlin.de

b Department of Chemistry, University of Oxford, Inorganic Chemistry Laboratory, South Parks Rd, Oxford, UK

c Institute of Technical Biochemistry, Universität Stuttgart, Allmandring 31, Stuttgart, Germany

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 H2-driven NADH cofactor regeneration even in the presence of O2, the co-substrate of monooxygenase.

Graphical abstract: H2-driven biotransformation of n-octane to 1-octanol by a recombinant Pseudomonas putida strain co-synthesizing an O2-tolerant hydrogenase and a P450 monooxygenase

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Article information

DOI
https://doi.org/10.1039/C5CC06078H
Article type
Communication
Submitted
21 Jul 2015
Accepted
11 Sep 2015
First published
11 Sep 2015
This article is Open Access
Creative Commons BY license

Chem. Commun., 2015,51, 16173-16175

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H2-driven biotransformation of n-octane to 1-octanol by a recombinant Pseudomonas putida strain co-synthesizing an O2-tolerant hydrogenase and a P450 monooxygenase

T. H. Lonsdale, L. Lauterbach, S. Honda Malca, B. M. Nestl, B. Hauer and O. Lenz, Chem. Commun., 2015, 51, 16173 DOI: 10.1039/C5CC06078H

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