Direct FeS cluster involvement in generation of a radical in lysine 2,3-aminomutase

N. J. Cosper, S. J. Booker, F. Ruzicka, P. A. Frey, R. A. Scott

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Abstract

Lysine 2,3-aminomutase (KAM) belongs to a class of enzymes that use FeS clusters and S-adenosyl-L-methionine to initiate radical-dependent chemistry. Selenium K-edge X-ray absorption spectroscopic analysis of KAM poised at various stages of catalysis, in the presence of selenomethionine or Se-adenosyl-L-selenomethionine, reveals that the cofactor is cleaved only in the presence of dithionite and the substrate analogue trans-4,5-dehydrolysine. A new Fourier transform peak at 2.7 Å, assigned as a Se - Fe interaction, appears concomitant with this cleavage. This is the first demonstration of a direct interaction of S-adenosyl-L-methionine, or its cleavage products, with the FeS cluster in this class of enzymes.

Original languageEnglish (US)
Pages (from-to)15668-15673
Number of pages6
JournalBiochemistry
Volume39
Issue number51
DOIs
StatePublished - Dec 26 2000

All Science Journal Classification (ASJC) codes

  • Biochemistry

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