Autor: |
Tai H; MOE Key Laboratory of Natural Resources of the Changbai Mountain and Functional Molecules, Department of Chemistry, Yanbian University, Park Road 977, Yanji, 133002, Jilin, China., Hirota S; Division of Materials Science, Graduate School of Science and Technology, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara, 630-0192, Japan. |
Jazyk: |
angličtina |
Zdroj: |
Chembiochem : a European journal of chemical biology [Chembiochem] 2020 Jun 02; Vol. 21 (11), pp. 1573-1581. Date of Electronic Publication: 2020 Apr 02. |
DOI: |
10.1002/cbic.202000058 |
Abstrakt: |
Hydrogenases (H 2 ase) catalyze the oxidation of dihydrogen and the reduction of protons with remarkable efficiency, thereby attracting considerable attention in the energy field due to their biotechnological potential. For this simple reaction, [NiFe] H 2 ase has developed a sophisticated but intricate mechanism with the heterolytic cleavage of dihydrogen, where its Ni-Fe active site exhibits various redox states. Recently, new spectroscopic and crystal structure studies of [NiFe] H 2 ases have been reported, providing significant insights into the catalytic reaction mechanism, hydrophobic gas-access tunnel, proton-transfer pathway, and electron-transfer pathway of [NiFe] H 2 ases. In addition, [NiFe] H 2 ases have been shown to play an important role in biofuel cell and solar dihydrogen production. This concept provides an overview of the biocatalytic reaction mechanism and biochemical application of [NiFe] H 2 ases based on the new findings. (© 2020 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.) |
Databáze: |
MEDLINE |
Externí odkaz: |
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