Recent advances on the structure and catalytic mechanism of hydrogenase.
- Author:
Jing-Jing LIU
1
;
Min-Nan LONG
Author Information
1. Institute of Microbiology and Marine Medicine, School of Life Sciences, Xiamen University, Xiamen 361005, China.
- Publication Type:Journal Article
- MeSH:
Catalysis;
Catalytic Domain;
Hydrogenase;
metabolism;
Iron-Sulfur Proteins;
metabolism;
Oxidation-Reduction
- From:
Chinese Journal of Biotechnology
2005;21(3):348-353
- CountryChina
- Language:Chinese
-
Abstract:
Hydrogenases are enzymes that catalyse the oxidation of hydrogen and the reduction of protons. It plays an important role in the process of biohydrogen production. According to the metal atoms within hydrogenase, it can be classified as NiFe-hydrogenase, Fe-hydrogenase and metal-free hydrogenase. The overwhelming majority of hydrogenases are metalloenzymes. The metal atoms are involved in the forming of active site and [Fe-S] clusters. The active site directly catalyzes the reduction of protons and the oxidation of hydrogen. The [Fe-S] clusters are involved in the transport of electrons between the H2-activating site and the redox partners of hydrogenase. Presently, the crystal structures of NiFe-hydrogenase and Fe-hydrogenase from a few kinds of microorganism have been revealed. The metal-free hydrogenase, characterized by the absence of [Fe-S] cluster and the presence of an iron-containing cofactor, shows a great diversity comparing with those of NiFe-hydrogenases and Fe-hydrogenases. Recent progress have also indicated the mechanisms of activation.
