Iron–Sulfur Cluster States of the Hydrogenase Maturase HydF
Author:
Affiliation:
1. Department of Chemistry and Biochemistry, Montana State University, Bozeman, Montana 59717, United States
Funder
Basic Energy Sciences
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.7b00735
Reference5 articles.
1. [FeFe]- and [NiFe]-hydrogenase diversity, mechanism, and maturation
2. Catalytic Turnover of [FeFe]-Hydrogenase Based on Single-Molecule Imaging
3. [FeFe]-Hydrogenase Maturation
4. A Redox Active [2Fe-2S] Cluster on the Hydrogenase Maturase HydF
5. Electron Spin Relaxation and Biochemical Characterization of the Hydrogenase Maturase HydF: Insights into [2Fe-2S] and [4Fe-4S] Cluster Communication and Hydrogenase Activation
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1. Role of Ammonia Lyases in the Synthesis of the Dithiomethylamine Ligand During [FeFe]-hydrogenase Maturation;Journal of Biological Chemistry;2024-09
2. HydG, the “dangler” iron, and catalytic production of free CO and CN−: implications for [FeFe]-hydrogenase maturation;Dalton Transactions;2021
3. H-cluster assembly intermediates built on HydF by the radical SAM enzymes HydE and HydG;JBIC Journal of Biological Inorganic Chemistry;2019-09
4. Overview of the Maturation Machinery of the H-Cluster of [FeFe]-Hydrogenases with a Focus on HydF;International Journal of Molecular Sciences;2018-10-11
5. Compositional and structural insights into the nature of the H-cluster precursor on HydF;Dalton Transactions;2018
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