The Aging-Associated Enzyme CLK-1 is a Member of the Carboxylate-Bridged Diiron Family of Proteins
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Behan and Lippard Biochemistry.pdf
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Author(s) •
Behan, Rachel K.
Lippard, Stephen J.
Date Issued
October 2010
Journal
Biochemistry
Publisher
American Chemical Society
Citation
Behan, Rachel K., and Stephen J. Lippard. “The Aging-Associated Enzyme CLK-1 Is a Member of the Carboxylate-Bridged Diiron Family of Proteins.” Biochemistry 49.45 (2010): 9679-9681.
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Author's final manuscript
Abstract
The aging-associated enzyme CLK-1 is proposed to be a member of the carboxylate-bridged diiron family of proteins. To evaluate this hypothesis and characterize the protein, we expressed soluble mouse CLK-1 (MCLK1) in Escherichia coli as a heterologous host. Using Mossbauer and EPR spectroscopy, we established that MCLK1 indeed belongs to this protein family. Biochemical analyses of the in vitro activity of MCLK1 with quinone substrates revealed that NADH can serve directly as a reductant for catalytic activation of dioxygen and substrate oxidation by the enzyme, with no requirement for an additional reductase protein component. The direct reaction of NADH with a diiron-containing oxidase enzyme has not previously been encountered for any member of the protein superfamily.
MIT Department
Massachusetts Institute of Technology. Department of Chemistry
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DOI of Published Version
https://doi.org/10.1021/bi101475z