Evidence for non‐cysteinyl coordination of the 2Fe‐2S cluster in Escherichia coli succinate dehydrogenase

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Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

1. 1Site-directed mutagenesis of conserved cysteine residues in Escherichia coli fumarate reductase: modification of the spectroscopic and electrochemical properties of the [2Fe-2S] cluster.1990 · 73 citations
2. 2Electrochemical and spectroscopic characterization of the conversion of the 7Fe into the 8Fe form of ferredoxin III from Desulfovibrio africanus. Identification of a [4Fe–4S] cluster with one non-cysteine ligand1989 · 125 citations
3. 3Nucleotide sequence encoding the iron-sulphur protein subunit of the succinate dehydrogenase of Escherichia coli1984 · 112 citations
4. 4Identification of active site residues of Escherichia coli fumarate reductase by site-directed mutagenesis1991 · 66 citations
5. 5Oxidation of reduced menaquinone by the fumarate reductase complex in Escherichia coli requires the hydrophobic FrdD peptide.1986 · 35 citations