Issue 47, 2020

Characterization of a putative sensory [FeFe]-hydrogenase provides new insight into the role of the active site architecture

Abstract

[FeFe]-hydrogenases are known for their high rates of hydrogen turnover, and are intensively studied in the context of biotechnological applications. Evolution has generated a plethora of different subclasses with widely different characteristics. The M2e subclass is phylogenetically distinct from previously characterized members of this enzyme family and its biological role is unknown. It features significant differences in domain- and active site architecture, and is most closely related to the putative sensory [FeFe]-hydrogenases. Here we report the first comprehensive biochemical and spectroscopical characterization of an M2e enzyme, derived from Thermoanaerobacter mathranii. As compared to other [FeFe]-hydrogenases characterized to-date, this enzyme displays an increased H2 affinity, higher activation enthalpies for H+/H2 interconversion, and unusual reactivity towards known hydrogenase inhibitors. These properties are related to differences in active site architecture between the M2e [FeFe]-hydrogenase and “prototypical” [FeFe]-hydrogenases. Thus, this study provides new insight into the role of this subclass in hydrogen metabolism and the influence of the active site pocket on the chemistry of the H-cluster.

Graphical abstract: Characterization of a putative sensory [FeFe]-hydrogenase provides new insight into the role of the active site architecture

Supplementary files

Article information

Article type
Edge Article
Submitted
15 6 2020
Accepted
19 9 2020
First published
21 9 2020
This article is Open Access

All publication charges for this article have been paid for by the Royal Society of Chemistry
Creative Commons BY license

Chem. Sci., 2020,11, 12789-12801

Characterization of a putative sensory [FeFe]-hydrogenase provides new insight into the role of the active site architecture

H. Land, A. Sekretareva, P. Huang, H. J. Redman, B. Németh, N. Polidori, L. S. Mészáros, M. Senger, S. T. Stripp and G. Berggren, Chem. Sci., 2020, 11, 12789 DOI: 10.1039/D0SC03319G

This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. You can use material from this article in other publications without requesting further permissions from the RSC, provided that the correct acknowledgement is given.

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