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Electron Transfer and Catalytic Control by the Iron−Sulfur Clusters in a Respiratory Enzyme,E.coliFumarate Reductase
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
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Evidence for reversible multiple redox transformations of [3Fe‐4S] clusters
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Succinate dehydrogenase and fumarate reductase from Escherichia coli
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Iron–sulfur clusters/semiquinones in Complex I
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Simple redox-linked proton-transfer design: new insights from structures of quinol-fumarate reductase
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Effect of cysteine to serine mutations on the properties of the [4Fe-4S] center in Escherichia coli fumarate reductase
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Reversible electrochemistry of fumarate reductase immobilized on an electrode surface. Direct voltammetric observations of redox centers and their participation in rapid catalytic electron transport
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[3Fe-4S] to [4Fe-4S] cluster conversion in Escherichia coli fumarate reductase by site-directed mutagenesis
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Oxidation-Reduction Potentials of Organic Systems.
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Direct Detection and Measurement of Electron Relays in a Multicentered Enzyme: Voltammetry of Electrode-Surface Films of E. coli Fumarate Reductase, an Iron−Sulfur Flavoprotein
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Architecture of Succinate Dehydrogenase and Reactive Oxygen Species Generation
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Structure of the Escherichia coli Fumarate Reductase Respiratory Complex
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