Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 127, Issue 19, Pages 6977-6989Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja043404q
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Funding
- Biotechnology and Biological Sciences Research Council [B19096] Funding Source: Medline
- NIGMS NIH HHS [GM 61606] Funding Source: Medline
- Biotechnology and Biological Sciences Research Council [B19096] Funding Source: researchfish
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Factors governing the efficacy of long-range electron relays in enzymes have been examined using protein film voltarnmetry 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.
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