Connecting [4Fe–4S] Clusters and Hemes – Towards Modeling the Active Site of Sulfite Reductase
Author:
Affiliation:
1. Department of Chemistry, University of Michigan, 930 N University, Ann Arbor, MI 48109
Publisher
Wiley
Subject
Inorganic Chemistry
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1002/ejic.201300308
Reference33 articles.
1. Structural and Functional Aspects of Metal Sites in Biology
2. Desulfovibrio desulfuricans iron hydrogenase: the structure shows unusual coordination to an active site Fe binuclear center
3. A functional Ni-Ni-[4Fe-4S] cluster in the monomeric acetyl-CoA synthase from Carboxydothermus hydrogenoformans
4. Sulfite Reductase Structure at 1.6 Å: Evolution and Catalysis for Reduction of Inorganic Anions
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3. Molecular understanding of heteronuclear active sites in heme–copper oxidases, nitric oxide reductases, and sulfite reductases through biomimetic modelling;Chemical Society Reviews;2021
4. Halide coordinated homoleptic [Fe4S4X4]2−and heteroleptic [Fe4S4X2Y2]2−clusters (X, Y = Cl, Br, I)—alternative preparations, structural analogies and spectroscopic properties in solution and solid state;Dalton Transactions;2016
5. Preface for Small-Molecule Activation: From Biological Principles to Energy Applications. Part 2: Small Molecules Related to the Global Nitrogen Cycle;Inorganic Chemistry;2015-10-05
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