Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 289, Issue 41, Pages 28095-28103Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.R114.588145
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Funding
- Biotechnology and Biological Sciences Research Council (BBSRC) [BB/K00817X/1, BB/J017787/1]
- Biotechnology and Biological Sciences Research Council [BB/J017787/1, BB/K00817X/1] Funding Source: researchfish
- BBSRC [BB/K00817X/1, BB/J017787/1] Funding Source: UKRI
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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.
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