The function of adenosylcobalamin in the mechanism of ribonucleoside triphosphate reductase from Lactobacillus leichmannii

Autor:	Christopher C. Lawrence, JoAnne Stubbe
Rok vydání:	1998
Předmět:	Free Radicals Stereochemistry Entropy Deoxyribonucleotides Ligands Biochemistry Catalysis Cofactor Analytical Chemistry chemistry.chemical_compound Allosteric Regulation Ribonucleotide Reductases medicine Moiety Nucleotide chemistry.chemical_classification biology Chemistry Ligand Electron Spin Resonance Spectroscopy Cobalt Biological Evolution Adenosylcobalamin Homolysis Kinetics Lactobacillus Dimethylbenzimidazole Ribonucleoside-triphosphate reductase Mutagenesis Site-Directed biology.protein Cobamides medicine.drug
Zdroj:	Current Opinion in Chemical Biology. 2:650-655
ISSN:	1367-5931
DOI:	10.1016/s1367-5931(98)80097-5
Popis:	Ribonucleoside triphosphate reductase from Lactobacillus leichmannii catalyzes the reduction of nucleotides to deoxynucleotides and uses adenosylcobalamin as a cofactor. transient protein-based thiyl radical is essential for catalysis. Studies directed toward the elucidation of the function of adenosylcobalamin during catalysis have shown that formation of the thiyl radical and 5′-deoxyadenosine occurs in a concerted fashion with CCo bond homolysis, that the homolysis is entropically and not enthalpically driven, that the dimethylbenzimidazole moiety of adenosylcobalamin is the axial ligand during catalysis, and that the CCo bond is reformed after every turnover.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9ae42d253e226ff293781a8310bbde14 https://doi.org/10.1016/s1367-5931(98)80097-5 Zobrazit plný text záznamu Full Text from ScienceDirect