Adenosylcobinamide, the Base-Free Analog of Coenzyme B12 (Adenosylcobalamin). 1.1 Probing the Role of the Axial 5,6-Dimethylbenzimidazole Base in Coenzyme B12 via Exogenous Axial Base Kassociation, ΔH, and ΔS Measurements plus a Critical Review of the Relevant Biochemical Literature
Adenosylcobinamide, the Base-Free Analog of Coenzyme B12 (Adenosylcobalamin). 1.1 Probing the Role of the Axial 5,6-Dimethylbenzimidazole Base in Coenzyme B12 via Exogenous Axial Base Kassociation, ΔH, and ΔS Measurements plus a Critical Review of the Relevant Biochemical Literature
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腺苷钴酰胺,辅酶 B12 的无碱基类似物(腺苷钴胺素) 1.1 通过外源轴向碱基结合、ΔH 和 ΔS 测量以及相关生化文献的批判性回顾探讨辅酶 B12 中轴向 5,6-二甲基苯并咪唑碱基的作用。
DOI:
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发表时间:
1996
期刊:
影响因子:
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通讯作者:
R. Finke
中科院分区:
文献类型:
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作者:
C. Garr;and Jeanne M. Sirovatka;R. Finke
Adenosylcobinamide (AdoCbi+BF4-), the base-free form of adenosylcobalamin (AdoCbl or coenzyme B12), has been studied with a series of 14 exogenous α-axial bases. Specifically, equilibrium association constants, Kassoc, as a function of temperature were measured, and thus their associated ΔH and ΔS were obtained. Bases studied include the following: (i) exogenous 1,5,6-trimethylbenzimidazole [analogous to adenosylcobalamin's intramolecularly appended 5,6-dimethylbenzimidazole base]; (ii) sterically encumbered phosphine bases (none of which showed detectable binding in dramatic contrast to studies of, for example, cobaloxime B12 “models”); and (iii) electronically increasingly donating, but isosteric, 4-substituted pyridine axial bases. The general trends from the present Kassoc studies are 2-fold: the more electron donating the base, the greater the Kassoc, and bulky bases bind weakly if at all. This paper also contains a tabular summary of the existing, non-Ado RCbi+ axial-base Kassoc literature plus th...