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Bioinorganic chemistry

Hydrogenase sophistication

Nature volume 397, pages 214–215 (1999)Cite this article

Hydrogenases, which catalyse the production and consumption of hydrogen gas, occupy a central place in the energy metabolism of anaerobic bacteria, and have probably done so since the earliest times of life on Earth1. There are two types, one of which — the iron-only [Fe]-hydrogenases — have been especially difficult to study because of their sensitivity to oxygen2.

Hydrogen is produced by many microbes under anaerobic conditions, and then consumed by others as a fuel1,2. The two types of hydrogenase known are the nickel-iron ([NiFe]) hydrogenases, the first structure of which was solved in 1995 (ref. 5) and which are used mostly for hydrogen consumption; and the [Fe]-hydrogenases, which are most frequently used for hydrogen production. It turns out that the overall structures of the [Fe]-hydrogenases are quite different to those of their [Ni-Fe] cousins, but some features are very similar and probably represent convergent evolution.

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Figure 1: General features of the [Fe]-hydrogenases from Clostridium pasteurianum and Desulfovibrio desulfuricans (not to scale), as determined by Peters et al.3 and Nicolet et al.4.

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  1. Division of Life Sciences, Kings College, London, W8 7AH, UK

    Richard Cammack

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Cammack, R. Hydrogenase sophistication. Nature 397, 214–215 (1999). https://doi.org/10.1038/16601

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