期刊
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
卷 611, 期 -, 页码 3-19出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2016.04.010
关键词
zinc; zinc ions; zinc biochemistry; zinc biophysics; zinc speciation
资金
- National Science Centre
- Polish Ministry of Science and Higher Education [2012/07/E/NZ1/01894, IP2012 018272]
- Biotechnology and Biological Sciences Research Council [BB/K001442/1]
- BBSRC [BB/K001442/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/K001442/1] Funding Source: researchfish
The solution and complexation chemistry of zinc ions is the basis for zinc biology. In living organisms, zinc is redox-inert and has only one valence state: Zn(II). Its coordination environment in proteins is limited by oxygen, nitrogen, and sulfur donors from the side chains of a few amino acids. In an estimated 10% of all human proteins, zinc has a catalytic or structural function and remains bound during the lifetime of the protein. However, in other proteins zinc ions bind reversibly with dissociation and association rates commensurate with the requirements in regulation, transport, transfer, sensing, signalling, and storage. In contrast to the extensive knowledge about zinc proteins, the coordination chemistry of the mobile zinc ions in these processes, i.e. when not bound to proteins, is virtually unexplored and the mechanisms of ligand exchange are poorly understood. Knowledge of the biological inorganic chemistry of zinc ions is essential for understanding its cellular biology and for designing complexes that deliver zinc to proteins and chelating agents that remove zinc from proteins, for detecting zinc ion species by qualitative and quantitative analysis, and for proper planning and execution of experiments involving zinc ions and nanoparticles such as zinc oxide (ZnO). In most investigations, reference is made to zinc or Zn2+ without full appreciation of how biological zinc ions are buffered and how the d-block cation Zn2+ differs from s-block cations such as Ca2+ with regard to significantly higher affinity for ligands, preference for the donor atoms of ligands, and coordination dynamics. Zinc needs to be tightly controlled. The interaction with low molecular weight ligands such as water and inorganic and organic anions is highly relevant to its biology but in contrast to its coordination in proteins has not been discussed in the biochemical literature. From the discussion in this article, it is becoming evident that zinc ion speciation is important in zinc biochemistry and for biological recognition as a variety of low molecular weight zinc complexes have already been implicated in biological processes, e.g. with ATP, glutathione, citrate, ethylenediaminedisuccinic acid, nicotianamine, or bacillithiol. (C) 2016 The Authors. Published by Elsevier Inc. This is an open access article under the CC BY license.
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