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对与莱氏乳杆菌核糖核苷酸还原酶结合的富含13C的辅酶B12的核磁共振观察。

NMR observations of 13C-enriched coenzyme B12 bound to the ribonucleotide reductase from Lactobacillus leichmannii.

作者信息

Brown Kenneth L, Li Jing, Zou Xiang

机构信息

Department of Chemistry and Biochemistry, Ohio University, Athens, Ohio 45701, USA.

出版信息

Inorg Chem. 2006 Nov 13;45(23):9172-4. doi: 10.1021/ic061385a.

Abstract

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.

摘要

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。

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