Biochemistry

Inactivation of Lactobacillus leichmannii ribonucleotide reductase by 2′, 2′-difluoro-2′-deoxycytidine 5′-triphosphate: Covalent modification

GJS Lohman, JA Stubbe

文献索引：Lohman, Gregory J.S.; Stubbe, Joanne Biochemistry, 2010 , vol. 49, # 7 p. 1404 - 1417

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被引用次数: 11

摘要

Ribonucleotide reductase (RNR) from Lactobacillus leichmannii, a 76 kDa monomer using adenosylcobalamin (AdoCbl) as a cofactor, catalyzes the conversion of nucleoside triphosphates to deoxynucleotides and is rapidly (< 30 s) inactivated by 1 equiv of 2′, 2′- difluoro-2′-deoxycytidine 5′-triphosphate (F2CTP).[1′-3H]-and [5-3H] F2CTP were synthesized and used independently to inactivate RNR. Sephadex G-50 chromatography ...