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

被引：87

作者：

Cosper, NJ

Booker, SJ

Ruzicka, F

Frey, PA

Scott, RA ^{[1
]}

机构：

[1] Univ Georgia, Dept Chem, Athens, GA 30602 USA

[2] Penn State Univ, Dept Biochem & Mol Biol, University Pk, PA 16802 USA

[3] Univ Wisconsin, Dept Biochem, Madison, WI 53705 USA

来源：

BIOCHEMISTRY | 2000年 / 39卷 / 51期

关键词：

D O I：

10.1021/bi0022184

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 Angstrom, 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.

引用

页码：15668 / 15673

页数：6

共 34 条

[21] Activation of the anaerobic ribonucleotide reductase from Escherichia coli - The essential role of the iron-sulfur center for S-adenosylmethionine reduction [J].