EPR Spectroscopic Studies of the Fe–S Clusters in the O2-Tolerant [NiFe]-Hydrogenase Hyd-1 from Escherichia coli and Characterization of the Unique [4Fe–3S] Cluster by HYSCORE
Author:
Affiliation:
1. Department of Chemistry and ‡Center for Advanced Electron Spin Resonance, Oxford University, South Parks Road, OX1 3QR Oxford, United Kingdom
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/ja307117y
Reference79 articles.
1. Occurrence, Classification, and Biological Function of Hydrogenases: An Overview
2. Direct comparison of the electrocatalytic oxidation of hydrogen by an enzyme and a platinum catalystElectronic supplementary information (ESI) available: Levich plots at 1% and 10% hydrogen, and a comparison of the effect of carbon monoxide on oxidation currents obtained at platinum and enzyme-modified electrodes. See http://www.rsc.org/suppdata/cc/b2/b201337a/
3. Structure/Function Relationships of [NiFe]- and [FeFe]-Hydrogenases
4. Crystal structure of the nickel–iron hydrogenase from Desulfovibrio gigas
5. New Method for the Spin Quantitation of [4Fe−4S]+ Clusters with S = 3/2. Application to the FS0 Center of the NarGHI Nitrate Reductase from Escherichia coli
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