Brown Kenneth L, Li Jing, Zou Xiang
Department of Chemistry and Biochemistry, Ohio University, Athens, Ohio 45701, USA.
Inorg Chem. 2006 Nov 13;45(23):9172-4. doi: 10.1021/ic061385a.
The 13C NMR resonance and one-bond 1H-13C coupling constants of coenzyme B12 enriched in 13C in the cobalt-bound carbon have been observed in the complex of the coenzyme with the B12-dependent ribonucleotide reductase from Lactobacillus leichmannii. Neither the 13C NMR chemical shift nor the 1H-13C coupling constants are significantly altered by binding of the coenzyme to the enzyme. The results suggest that ground-state Co-C bond distortion is not utilized by this enzyme to activate coenzyme B12 for C-Co bond homolysis.
在辅酶与来自赖氏乳杆菌的维生素B12依赖性核糖核苷酸还原酶的复合物中,已观察到在与钴结合的碳中富含13C的辅酶B12的13C核磁共振共振和一键1H-13C耦合常数。辅酶与酶的结合并不会显著改变13C核磁共振化学位移或1H-13C耦合常数。结果表明,这种酶不会利用基态Co-C键畸变来激活辅酶B12进行C-Co键均裂。