X 射线吸收光谱法研究蜡样芽胞杆菌金属β-内酰胺酶 BcII 中金属结合部位的物种形成。
X-ray absorption spectroscopy of metal site speciation in the metallo-β-lactamase BcII from Bacillus cereus.
机构信息
Department of Chemistry and Biochemistry, Miami University, Oxford, OH 45056, United States.
出版信息
J Inorg Biochem. 2012 Jun;111:182-6. doi: 10.1016/j.jinorgbio.2011.12.013. Epub 2012 Jan 31.
Abstract
Cobalt and zinc binding by the subclass B1 metallo-β-lactamase BcII from Bacillus cereus is examined by X-ray absorption spectroscopy, at various levels of metal loading. The data show that a significant amount of the dinuclear enzyme is formed, even at substoichiometric levels of metal loading, whether the added metal is Zn(II) or Co(II). Increasing metal addition, from 0.5 to 1.0 to 2.0eq/mol of enzyme, are shown to result in a more ordered active site. While Zn(II) appears to show no preference for the Zn(1) (3H) or Zn(2) (DCH) sites, the extended X-ray absorption fine structure (EXAFS) suggests that Co(II) shows a slight preference for the DCH site at low levels of added Co(II). The results are discussed in the context of similar metal-binding studies of other B1 metallo-β-lactamases.
摘要
采用 X 射线吸收光谱法，在不同的金属负载水平下，研究了来自蜡状芽孢杆菌的 B 类亚家族 B1 金属β-内酰胺酶 BcII 对钴和锌的结合。数据表明，即使在亚化学计量的金属负载水平下，也会形成大量的双核酶，无论添加的金属是 Zn(II) 还是 Co(II)。结果表明，随着金属添加量从 0.5 增加到 1.0 再增加到 2.0eq/mol 的酶，活性位点的有序性增加。虽然 Zn(II) 似乎对 Zn(1) (3H) 或 Zn(2) (DCH) 位点没有偏好，但扩展 X 射线吸收精细结构 (EXAFS) 表明，在低水平添加 Co(II) 时，Co(II) 对 DCH 位点略有偏好。结果在讨论其他 B1 金属β-内酰胺酶的类似金属结合研究时进行了讨论。
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