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Metal preferences and metallation.

ABSTRACT: 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 ∼ 25% acquiring preassembled metal cofactors. The remaining ∼ 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.

SUBMITTER: Foster AW

PROVIDER: S-EPMC4192464 | biostudies-literature | 2014 Oct

REPOSITORIES: biostudies-literature

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Metal preferences and metallation.

Foster Andrew W AW Osman Deenah D Robinson Nigel J NJ

The Journal of biological chemistry 20140826 41

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 ∼ 25% acquiring preassembled metal cofactors. The remaining ∼ 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, magne ...[more]

PMID: 25160626

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Metal preferences and metallation.

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Metal preferences and metallation.

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