Extended X-ray Absorption Fine Structure Analysis of Coenzyme B12 Bound to Methylmalonyl-Coenzyme A Mutase Using Global Mapping Techniques
| Autor: | Eva M. Scheuring, Ruma Banerjee, Mark R. Chance, Rugmini Padmakumar |
|---|---|
| Rok vydání: | 1997 |
| Předmět: |
chemistry.chemical_classification
Reaction mechanism Extended X-ray absorption fine structure biology Stereochemistry Substrate (chemistry) General Chemistry medicine.disease_cause Biochemistry Catalysis Crystallography Colloid and Surface Chemistry Enzyme Mutase chemistry medicine biology.protein Methionine synthase Escherichia coli Histidine |
| Zdroj: | Journal of the American Chemical Society. 119:12192-12200 |
| ISSN: | 1520-5126 0002-7863 |
| Popis: | The two available crystallographic structures of cobalamin dependent enzymes, the 27 kDa fragment of the methylcobalamin-dependent enzyme, methionine synthase, from Escherichia coli [Drennan, C. L. et al. Science 1994, 266, 1669] and the 5‘-deoxyadenosylcobalamin-dependent enzyme methylmalonyl-coenzyme A mutase from Propionibacterium shermanii [Mancia, F. et al. Structure 1996, 4, 339], show striking similarities despite the differences in reaction mechanism. In particular, the 5,6-dimethylbenzimidazole group is detached and replaced by a histidine group of the enzyme. Here we present an analysis of Extended X-ray Absorption Fine Structure (EXAFS) spectroscopic data for both 5‘-deoxyadenosylcobalamin and aquocobalamin bound to methylmalonyl-coenzyme A mutase in the absence of substrate. The analysis is conducted with a suite of programs called AUTOFIT 1.0 [Chance, et al. Biochemistry 1996, 35, 9014], which allows an evenhanded comparison of the goodness-of-fit of the EXAFS data to a varied grid of simulat... |
| Databáze: | OpenAIRE |
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