Mössbauer evidence for exchange-coupled siroheme and [4Fe-4S] prosthetic groups in Escherichia coli sulfite reductase. Studies of the reduced states and of a nitrite turnover complex.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference25 articles.
1. Mechanisms of Oxidizing Enzymes;Siegel,1978
2. Escherichia coli sulfite reductase hemoprotein subunit. Prosthetic groups, catalytic parameters, and ligand complexes.
3. Electron paramagnetic resonance and optical spectroscopic evidence for interaction between siroheme and iron sulfide (Fe4S4) prosthetic groups in Escherichia coli sulfite reductase hemoprotein subunit
4. Electron paramagnetic resonance and optical evidence for interaction between siroheme and the tetranuclear iron-sulfur center (Fe4S4) prosthetic groups in complexes of Escherichia coli sulfite reductase hemoprotein with added ligands
5. Characterization of complexes between Escherichia coli sulfite reductase hemoprotein subunit and its substrates sulfite and nitrite
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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
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