PMID:15884941
| Citation |
Hudson, JM, Heffron, K, Kotlyar, V, Sher, Y, Maklashina, E, Cecchini, G and Armstrong, FA (2005) Electron transfer and catalytic control by the iron-sulfur clusters in a respiratory enzyme, E. coli fumarate reductase. J. Am. Chem. Soc. 127:6977-89 |
|---|---|
| Abstract |
Factors governing the efficacy of long-range electron relays in enzymes have been examined using protein film voltammetry in conjunction with site-directed mutagenesis. Investigations of the fumarate reductase from Escherichia coli, in which three Fe-S clusters relay electrons over more than 30 A, lead to the conclusion that varying the medial [4Fe-4S] cluster potential over a 100 mV range does not have a significant effect on the inherent kinetics of electron transfer to and from the active-site flavin. The results support a proposal that the reduction potential of an individual electron relay site in a multicentered enzyme is not a strong determinant of activity; instead, as deduced from the potential dependence of catalytic electron transfer, electron flow through the intramolecular relay is rapid and reversible, and even uphill steps do not limit the catalytic rate. |
| Links |
PubMed Online version:10.1021/ja043404q |
| Keywords |
Amino Acid Sequence; Catalysis; Electrochemistry; Escherichia coli/enzymology; Flavins/chemistry; Flavins/metabolism; Iron-Sulfur Proteins/chemistry; Iron-Sulfur Proteins/genetics; Iron-Sulfur Proteins/metabolism; Kinetics; Models, Molecular; Mutagenesis, Site-Directed; Mutation, Missense; Oxidation-Reduction; Sequence Alignment; Structure-Activity Relationship; Succinate Dehydrogenase/chemistry; Succinate Dehydrogenase/genetics; Succinate Dehydrogenase/metabolism |
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