Issue 48, 2017

Chalcogenide substitution in the [2Fe] cluster of [FeFe]-hydrogenases conserves high enzymatic activity

Abstract

[FeFe]-Hydrogenases efficiently catalyze the uptake and evolution of H2 due to the presence of an inorganic [6Fe–6S]-cofactor (H-cluster). This cofactor is comprised of a [4Fe–4S] cluster coupled to a unique [2Fe] cluster where the catalytic turnover of H2/H+ takes place. We herein report on the synthesis of a selenium substituted [2Fe] cluster [Fe2{μ(SeCH2)2NH}(CO)4(CN)2]2− (ADSe) and its successful in vitro integration into the native protein scaffold of [FeFe]-hydrogenases HydA1 from Chlamydomonas reinhardtii and CpI from Clostridium pasteurianum yielding fully active enzymes (HydA1-ADSe and CpI-ADSe). FT-IR spectroscopy and X-ray structure analysis confirmed the presence of structurally intact ADSe at the active site. Electrochemical assays reveal that the selenium containing enzymes are more biased towards hydrogen production than their native counterparts. In contrast to previous chalcogenide exchange studies, the S to Se exchange herein is not based on a simple reconstitution approach using ionic cluster constituents but on the in vitro maturation with a pre-synthesized selenium-containing [2Fe] mimic. The combination of biological and chemical methods allowed for the creation of a novel [FeFe]-hydrogenase with a [2Fe2Se]-active site which confers individual catalytic features.

Graphical abstract: Chalcogenide substitution in the [2Fe] cluster of [FeFe]-hydrogenases conserves high enzymatic activity

Supplementary files

Article information

Article type
Paper
Submitted
09 Oct 2017
Accepted
16 Nov 2017
First published
16 Nov 2017

Dalton Trans., 2017,46, 16947-16958

Chalcogenide substitution in the [2Fe] cluster of [FeFe]-hydrogenases conserves high enzymatic activity

L. Kertess, F. Wittkamp, C. Sommer, J. Esselborn, O. Rüdiger, E. J. Reijerse, E. Hofmann, W. Lubitz, M. Winkler, T. Happe and U.-P. Apfel, Dalton Trans., 2017, 46, 16947 DOI: 10.1039/C7DT03785F

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