The DOI matches its Crossref record; 35 of the 35 references it cites were found in a registry or an index.
Unification of the Copper(I) Binding Affinities of the Metallo-chaperones Atx1, Atox1, and Related Proteins
Open accessAbstract
Literature estimates of metal-protein affinities are widely scattered for many systems, as highlighted by the class of metallo-chaperone proteins, which includes human Atox1. The discrepancies may be attributed to unreliable detection probes and/or inconsistent affinity standards. In this study, application of the four Cu(I) ligand probes bicinchoninate, bathocuproine disulfonate, dithiothreitol (Dtt), and glutathione (GSH) is reviewed, and their Cu(I) affinities are re-estimated and unified. Excess bicinchoninate or bathocuproine disulfonate reacts with Cu(I) to yield distinct 1:2 chromatophoric complexes [Cu(I)L(2)](3-) with formation constants β(2) = 10(17.2) and 10(19.8) m(-2), respectively. These constants do not depend on proton concentration for pH ≥7.0. Consequently, they are a pair of complementary and stable probes capable of detecting free Cu(+) concentrations from 10(-12) to 10(-19) m. Dtt binds Cu(I) with K(D) ∼10(-15) m at pH 7, but it is air-sensitive, and its Cu(I) affinity varies with pH. The Cu(I) binding properties of Atox1 and related proteins (including the fifth and sixth domains at the N terminus of the Wilson protein ATP7B) were assessed with these probes. The results demonstrate the following: (i) their use permits the stoichiometry of high affinity Cu(I) binding and the individual quantitative affinities (K(D) values) to be determined reliably via noncompetitive and competitive reactions, respectively; (ii) the scattered literature values are unified by using reliable probes on a unified scale; and (iii) Atox1-type proteins bind Cu(I) with sub-femtomolar affinities, consistent with tight control of labile Cu(+) concentrations in living cells.
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Cited by
Członkowska, A., Litwin, T., Dusek, P., Ferenci, P., Lutsenko, S., Medici, V., Rybakowski, J. K., Weiss, K. H., & Schilsky, M. L. (2018) · Nature Reviews Disease Primers · doi:10.1038/s41572-018-0018-3 · Cited by 913
Synthetic fluorescent probes for studying copper in biological systems
Cotruvo, Jr., Aron, A. T., Ramos-Torres, K. M., & Chang, C. J. (2015) · Chemical Society Reviews · doi:10.1039/c4cs00346b · Cited by 558
Charrier, J. G., & Anastasio, C. (2012) · Atmospheric Chemistry and Physics · doi:10.5194/acp-12-9321-2012 · Cited by 473
Cu Homeostasis in Bacteria: The Ins and Outs
Andrei, A., Öztürk, Y., Khalfaoui-Hassani, B., Rauch, J., Marckmann, D., Trasnea, P.-I., Daldal, F., & Koch, H.-G. (2020) · Membranes · doi:10.3390/membranes10090242 · Cited by 153
Bacterial sensors define intracellular free energies for correct enzyme metalation
Osman, D., Martini, M. A., Foster, A. W., Chen, J., Scott, A. J. P., Morton, R. J., Steed, J. W., Lurie-Luke, E., Huggins, T. G., Lawrence, A. D., et al. (2019) · Nature Chemical Biology · doi:10.1038/s41589-018-0211-4 · Cited by 147
Metadata
- Authors
- Xiao, Z., Brose, J., Schimo, S., Ackland, S. M., La Fontaine, S., & Wedd, A. G.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2011-04
- Volume
- 286
- Issue
- 13
- Pages
- 11047-11055
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1980099457
- Cited by
- 258
- References
- 35
- FWCI
- 16.23
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Xiao, Z., Brose, J., Schimo, S., Ackland, S. M., La Fontaine, S., & Wedd, A. G. (2011). Unification of the Copper(I) Binding Affinities of the Metallo-chaperones Atx1, Atox1, and Related Proteins. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m110.213074
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