The DOI matches its Crossref record; 98 of the 98 references it cites were found in a registry or an index.
Metal Preferences and Metallation
Open accessAbstract
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.
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Cites
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“Importantly, the absolute metal preferences, as reflected in KMetal values of InrS (nickel-responsive efflux derepressor), CoaR (cobalt-responsive efflux activator), and ZiaR and Zur (zinc-responsive efflux derepressor and influx corepressor, respectively) (61, 83, 86, 87), do not universally match their metal specifi…”
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Self-citationOrder of Stability of Metal Complexes
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How do bacterial cells ensure that metalloproteins get the correct metal?
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Self-citationTetrapyrrole Biosynthesis in Higher Plants
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Metal homeostasis and resistance in bacteria
Chandrangsu, P., Rensing, C., & Helmann, J. D. (2017) · Nature Reviews Microbiology · doi:10.1038/nrmicro.2017.15 · Cited by 812
Khezerlou, A., Alizadeh-Sani, M., Azizi-Lalabadi, M., & Ehsani, A. (2018) · Microbial Pathogenesis · doi:10.1016/j.micpath.2018.08.008 · Cited by 404
Iron homeostasis in plants and its crosstalk with copper, zinc, and manganese
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Bacterial Strategies to Maintain Zinc Metallostasis at the Host-Pathogen Interface
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Top-down characterization of endogenous protein complexes with native proteomics
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Metadata
- Authors
- Foster, A. W., Osman, D., & Robinson, N. J.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2014-10
- Volume
- 289
- Issue
- 41
- Pages
- 28095-28103
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2019190661
- Cited by
- 379
- References
- 98
- FWCI
- 24.91
- Type
- journal article
- Language
- en
- Open access
- hybrid
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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