Journal
STRUCTURE
Volume 24, Issue 2, Pages 285-292Publisher
CELL PRESS
DOI: 10.1016/j.str.2015.11.010
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Funding
- German Ministry of Science and Education (BMBF)
- Helmholtz Zentrum Berlin fur Materialien und Energie
- Freie Universitat Berlin
- Humboldt-Universitat zu Berlin
- Max-Delbruck-Centrum
- Leibniz-Institut fur Molekulare Pharmakologie
- Cluster of Excellence Unifying Concepts in Catalysis (UniCat)
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A novel group of bacterial [NiFe]-hydrogenases is responsible for high-affinity H-2 uptake from the troposphere, and is therefore thought to play an important role in the global H-2 cycle. Here we present the first crystal structure at 2.85-angstrom resolution of such an actinobacterial-type hydrogenase (AH), which was isolated from the dihydrogen oxidizing bacterium, Ralstonia eutropha. The enzyme has a dimeric structure carrying two active [NiFe] sites that are interconnected by six [4Fe4S] clusters over a range of approximately 90 angstrom. Unlike most other [NiFe]-hydrogenases, the [4Fe4S] cluster proximal to the [NiFe] site is coordinated by three cysteines and one aspartate. Mutagenesis experiments revealed that this aspartate residue is related to the apparent O-2 insensitivity of the AH. Our data provide first structural insight into specialized hydrogenases that are supposed to consume atmospheric H-2 under challenging conditions, i.e. at high O-2 concentration and wide temperature and pH ranges.
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