Literature DB >> 17083212

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

Kenneth L Brown1, Jing Li, Xiang Zou.   

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.

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Year:  2006        PMID： 17083212      PMCID： PMC2517903          DOI： 10.1021/ic061385a

Source DB:  PubMed          Journal:  Inorg Chem        ISSN： 0020-1669            Impact factor:   5.165


  26 in total

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Authors:  Amanda J Brooks; Monica Vlasie; Ruma Banerjee; Thomas C Brunold
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Authors:  J S Trommel; K Warncke; L G Marzilli
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7.  Thermodynamic and kinetic characterization of Co-C bond homolysis catalyzed by coenzyme B(12)-dependent methylmalonyl-CoA mutase.

Authors:  S Chowdhury; R Banerjee
Journal:  Biochemistry       Date:  2000-07-11       Impact factor: 3.162

8.  How coenzyme B12 radicals are generated: the crystal structure of methylmalonyl-coenzyme A mutase at 2 A resolution.

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9.  Cloning, sequencing, and expression of the adenosylcobalamin-dependent ribonucleotide reductase from Lactobacillus leichmannii.

Authors:  S Booker; J Stubbe
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10.  Spectroscopic and computational studies on the adenosylcobalamin-dependent methylmalonyl-CoA mutase: evaluation of enzymatic contributions to Co-C bond activation in the Co3+ ground state.

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Journal:  J Am Chem Soc       Date:  2004-07-07       Impact factor: 15.419
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