Martinez-Gomez N Cecilia, Poyner Russell R, Mansoorabadi Steven O, Reed George H, Downs Diana M
Department of Bacteriology, University of Wisconsin, Madison, Wisconsin 53706, USA.
Biochemistry. 2009 Jan 20;48(2):217-9. doi: 10.1021/bi802154j.
ThiC is an [4Fe-4S] cluster protein that catalyzes the formation of 4-amino-5-hydroxymethyl-2-methylpyrimidine. EPR spectroscopic studies demonstrate that, upon interaction with AdoMet, active ThiC from Salmonella enterica generates a persistent free radical on the alpha-carbon of an amino acid residue. The EPR properties of the radical are consistent with any residue other than a Gly or Ala. Exposure to oxygen was accompanied by a fission of the radical-carrying polypeptide chain between the Gly436 and His437 residues in ThiC. Regardless of whether the backbone radical is part of the catalytic machinery, its presence provides evidence that ThiC employs free radical chemistry as expected for radical SAM enzymes.
硫胺素合成酶C(ThiC)是一种含[4Fe-4S]簇的蛋白质,可催化4-氨基-5-羟甲基-2-甲基嘧啶的形成。电子顺磁共振(EPR)光谱研究表明,来自肠炎沙门氏菌的活性ThiC与腺苷甲硫氨酸(AdoMet)相互作用时,会在氨基酸残基的α-碳上产生一个持久的自由基。该自由基的EPR特性与除甘氨酸(Gly)或丙氨酸(Ala)以外的任何残基一致。暴露于氧气时,ThiC中Gly436和His437残基之间携带自由基的多肽链会发生断裂。无论主链自由基是否是催化机制的一部分,它的存在都证明ThiC如预期的那样采用自由基化学,这是自由基S-腺苷甲硫氨酸(SAM)酶的特征。