Hydrogen bonding effect between active site and protein environment on catalysis performance in H2-producing [NiFe] hydrogenases
Author:
Affiliation:
1. School of Chemistry
2. Faculty of Science
3. Monash University
4. Clayton
5. Australia
6. Department of Chemistry and Biotechnology
7. Swinburne University of Technology
8. Hawthorn
9. VIC 3122
Abstract
The interaction between the active site and the surrounding protein environment plays a fundamental role in the hydrogen evolution reaction (HER) in [NiFe] hydrogenases.
Funder
Centre of Excellence for Electromaterials Science, Australian Research Council
Publisher
Royal Society of Chemistry (RSC)
Subject
Physical and Theoretical Chemistry,General Physics and Astronomy
Link
http://pubs.rsc.org/en/content/articlepdf/2018/CP/C7CP07685A
Reference78 articles.
1. Crystal structure of the nickel–iron hydrogenase from Desulfovibrio gigas
2. Structure of the [NiFe] Hydrogenase Active Site: Evidence for Biologically Uncommon Fe Ligands
3. Nature and Electronic Structure of the Ni-X Dinuclear Center of Desulfovibrio gigas Hydrogenase. Implications for the Enzymatic Mechanism
4. Interfacial processes involving electrocatalytic evolution and oxidation of H2, and the role of chemisorbed H
5. Trends in the Exchange Current for Hydrogen Evolution
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