Journal
CHEMISTRY LETTERS
Volume 49, Issue 2, Pages 164-173Publisher
CHEMICAL SOC JAPAN
DOI: 10.1246/cl.190814
Keywords
[NiFe]-hydrogenase; O-2-tolerance; Reaction mechanism
Categories
Funding
- MEXT KAKENHI [18H05516]
- JSPS KAKENHI [19H00984]
- JST CREST grant [JPMJCR12M4]
- JSPS KAKENHI Returning Researcher Development Research [16K21748]
- Kinoshita Kinen Jigyo
- Grants-in-Aid for Scientific Research [19H00984, 16K21748, 18H05516] Funding Source: KAKEN
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Hydrogenases control the proton concentration in cells, which is an essential function for hydrogen metabolism in several microorganisms. Some [NiFe]-hydrogenases are catalytically active under air and are thus of great interest for developing bio-inspired synthetic models and new devices for clean energy conversion. Here, we provide an overview of the structural basis of the reaction mechanism of [NiFe]-hydrogenases, and the recent development of a new assay method which may uncover hidden properties of hydrogenases.
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