doi: 10.1021/bi0022184.
Direct FeS cluster involvement in generation of a radical in lysine 2,3-aminomutase
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- PMID: 11123891
- DOI: 10.1021/bi0022184
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Direct FeS cluster involvement in generation of a radical in lysine 2,3-aminomutase
Biochemistry.
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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 A, 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.
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