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

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 regenerati...

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Veröffentlicht in:Chemical communications (Cambridge, England) England), 2015-10, Vol.51 (90), p.16173-16175
Hauptverfasser: Lonsdale, Thomas H., Lauterbach, Lars, Honda Malca, Sumire, Nestl, Bettina M., Hauer, Bernhard, Lenz, Oliver
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container_end_page 16175
container_issue 90
container_start_page 16173
container_title Chemical communications (Cambridge, England)
container_volume 51
creator Lonsdale, Thomas H.
Lauterbach, Lars
Honda Malca, Sumire
Nestl, Bettina M.
Hauer, Bernhard
Lenz, Oliver
description 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.
doi_str_mv 10.1039/C5CC06078H
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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
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