Metal Preferences and Metallation

被引:281
作者
Foster, Andrew W.
Osman, Deenah
Robinson, Nigel J. [1 ]
机构
[1] Univ Durham, Dept Chem, Durham DH1 3LE, England
基金
英国生物技术与生命科学研究理事会;
关键词
C-TERMINAL DOMAIN; ESCHERICHIA-COLI; COPPER CHAPERONE; TRANSCRIPTIONAL ACTIVATOR; INTRACELLULAR MAGNESIUM; MONOTHIOL GLUTAREDOXINS; MOLYBDENUM COFACTOR; ION SELECTIVITY; BINDING SITES; ZINC;
D O I
10.1074/jbc.R114.588145
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The metal binding preferences of most metalloproteins do not match their metal requirements. Thus, metallation of an estimated 30% of metalloenzymes is aided by metal delivery systems, with similar to 25% acquiring preassembled metal cofactors. The remaining similar to 70% are presumed to compete for metals from buffered metal pools. Metallation is further aided by maintaining the relative concentrations of these pools as an inverse function of the stabilities of the respective metal complexes. For example, magnesium enzymes always prefer to bind zinc, and these metals dominate the metalloenzymes without metal delivery systems. Therefore, the buffered concentration of zinc is held at least a million-fold below magnesium inside most cells.
引用
收藏
页码:28095 / 28103
页数:9
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