Metal Preferences and Metallation

Foster, Andrew W.; Osman, Deenah; Robinson, Nigel J.

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 pre-assembled 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.

Citation

Foster, A. W., Osman, D., & Robinson, N. J. (2014). Metal Preferences and Metallation. Journal of Biological Chemistry, 289(41), 28095-28103. https://doi.org/10.1074/jbc.r114.588145

• Journal Article Type: Article
• Online Publication Date: Aug 26, 2014
• Publication Date: Oct 10, 2014
• Deposit Date: Sep 11, 2014
• Publicly Available Date: Sep 11, 2014
• Journal: Journal of Biological Chemistry
• Print ISSN: 0021-9258
• Electronic ISSN: 1083-351X
• Publisher: American Society for Biochemistry and Molecular Biology
• Peer Reviewed: Peer Reviewed
• Volume: 289
• Issue: 41
• Pages: 28095-28103
• DOI: https://doi.org/10.1074/jbc.r114.588145
• Keywords: Copper, Iron, Manganese, Nickel, Zinc, Irving-Williams Series, Metal sensors, Metallochaperone, Metalloenzymes, Polydisperse, Buffer.
• Public URL: https://durham-repository.worktribe.com/output/1454202
• Related Public URLs: http://www.ncbi.nlm.nih.gov/pubmed/25160626