The DOI matches its Crossref record; 36 of the 36 references it cites were found in a registry or an index.
Aqueous Coordination Chemistry of Quinoline-Based Fluorescence Probes for the Biological Chemistry of Zinc
Abstract
Metal-specific fluorescence probes are of increasing importance in understanding the neurobiology and general cell biology of zinc. Several quinoline-based compounds such as TSQ and zinquin have been employed to detect zinc in fluorescence microscopy experiments in vivo; however, the aqueous solution chemistry remains equivocal. In some cases, this family of probes is said to reveal labile pools of Zn(II) inside the cell, yet in other cases, these probes are suggested to remove Zn(II) from tightly bound sites in proteins. Since the binding modes, coordination numbers, and thermodynamics of zinc−zinquin interactions in aqueous solution have not been established, these proposals are difficult to distinguish. Here we show that, under physiological conditions, the various forms of zinquin bind Zn(II) with a high degree of cooperativity forming 2:1 complexes. Potentiometric, UV−visible, and fluorescence methods all yield an overall binding constant of log K = 13.5 under physiological conditions. To put this number in perspective with other Zn chelators and biological ligands, we compare the calculated so-called p M values (−log[Zn(II)] free ) for a series of compounds with different stoichiometries under a typical condition. The pZn value for zinquin (9.3) is similar to that of EGTA (9.5) but much smaller than the value for carbonic anhydrase (12.4) or EDTA (14.3) and, thus, serves as a useful gauge for comparing zinc affinities. With respect to in vivo applications of zinquin, such as intracellular fluorescence microscopy studies, we find that the typical detection limit for free Zn(II) in aqueous solution is 4 pM, or 0.3 parts per trillion, at pH 7.2. These results have implications for the availability of zinc in various intracellular compartments.
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Cites
The biochemical basis of zinc physiology
Vallee, B. L., & Falchuk, K. H. (1993) · Physiological Reviews · doi:10.1152/physrev.1993.73.1.79 · Cited by 2,990
Determination of the equivalence point in potentiometric titrations. Part II
Gran, G. (1952) · The Analyst · doi:10.1039/an9527700661 · Cited by 2,941
Fluorescent indicators for cytosolic calcium based on rhodamine and fluorescein chromophores
Minta, A., Kao, J. P. Y., & Tsien, R. Y. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83165-9 · Cited by 1,613
Neurobiology of Zinc and Zinc-Containing Neurons
Frederickson, C. J. (1989) · International Review of Neurobiology · doi:10.1016/s0074-7742(08)60279-2 · Cited by 1,075
Buffers for pH and Metal Ion Control.
Perrin, D. D., & Dempsey, B. (1975) · Journal of AOAC INTERNATIONAL · doi:10.1093/jaoac/58.4.864 · Cited by 872
Choi, D. W., & Koh, J. Y. (1998) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.21.1.347 · Cited by 752
The elusive function of metallothioneins
Palmiter, R. D. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.15.8428 · Cited by 679
Computational Methods for the Determination of Formation Constants
(1985) · Springer eBooks · doi:10.1007/978-1-4684-4934-1 · Cited by 621
Elimination of zinc from synaptic vesicles in the intact mouse brain by disruption of the ZnT 3 gene
Cole, T. B., Wenzel, H. J., Kafer, K. E., Schwartzkroin, P. A., & Palmiter, R. D. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.4.1716 · Cited by 545
Frederickson, C. J., Kasarskis, E. J., Ringo, D., & Frederickson, R. E. (1987) · Journal of Neuroscience Methods · doi:10.1016/0165-0270(87)90042-2 · Cited by 527
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Femtomolar Sensitivity of Metalloregulatory Proteins Controlling Zinc Homeostasis
Outten, C. E., & O'Halloran, A. T. V. (2001) · Science · doi:10.1126/science.1060331 · Cited by 1,489
Jiang, P., & Guo, Z. (2004) · Coordination Chemistry Reviews · doi:10.1016/j.cct.2003.10.013 · Cited by 989
Small-Molecule Fluorescent Sensors for Investigating Zinc Metalloneurochemistry
Nolan, E. M., & Lippard, S. J. (2009) · Accounts of Chemical Research · doi:10.1021/ar8001409 · Cited by 620
Gee, K. R., Zhou, Z.-L., Qian, W.-J., & Kennedy, R. (2002) · Journal of the American Chemical Society · doi:10.1021/ja011774y · Cited by 406
Concerted action of zinc and ProSAP/Shank in synaptogenesis and synapse maturation
Grabrucker, A. M., Knight, M. J., Proepper, C., Bockmann, J., Joubert, M., Rowan, M., Nienhaus, G. U., Garner, C. C., Bowie, J. U., Kreutz, M. R., et al. (2011) · The EMBO Journal · doi:10.1038/emboj.2010.336 · Cited by 228
Storr, T., Merkel, M., Song-Zhao, G. X., Scott, L. E., Green, D. E., Bowen, M. L., Thompson, K. H., Patrick, B. O., Schugar, H. J., & Orvig, C. (2007) · Journal of the American Chemical Society · doi:10.1021/ja068965r · Cited by 156
Talmard, C., Bouzan, A., & Faller, P. (2007) · Biochemistry · doi:10.1021/bi701355j · Cited by 111
High-Throughput Screen for Identifying Small Molecules That Target Fungal Zinc Homeostasis
Simm, C., Luan, C.-H., Weiss, E., & O'Halloran, T. (2011) · PLoS ONE · doi:10.1371/journal.pone.0025136 · Cited by 34
Self-citationCohrt, K. A. O., Marín, L., Kjellerup, L., Clausen, J. D., Dalby-Brown, W., Calera, J. A., & Winther, A.-M. L. (2018) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.02024-17 · Cited by 32
Metadata
- Authors
- Fahrni, C. J., & O'Halloran, T. V.
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 1999-11-30
- Volume
- 121
- Issue
- 49
- Pages
- 11448-11458
- ISSN
- 0002-7863 (ISSN-L)
- 1520-5126
- OpenAlex
- W1974194549
- Cited by
- 332
- References
- 36
- FWCI
- 7.04
- Type
- journal article
- Language
- en
- Open access
- closed
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