Metallomics in China

Hongzhe Sun

Hongzhe Sun, Professor of Chemistry at the University of Hong Kong obtained his PhD from the University of London in 1996. He undertook postdoctoral research at the University of Edinburgh investigating interactions of metallodrug with proteins. His research interests focus on metallodrugs and metalloproteins, inorganic structural biology and metallomics. He is a member of the editorial board of Metallomics, and a series editor of Metallobiology (RSC).

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About one quarter to one third of proteins in a proteome are found to be metalloproteins and metal-binding proteins. Matching metals to proteins (and other biomolecules) on a proteome-wide scale is an integral part of metallomics. As an emerging area, metallomics has rapidly been recognized in China^1,2 and significant progress has been made in recent years. A “seminar on metallomics and metalloproteomics” organized by Professors Zhifang Chai and Chunyong Chen in May 2008, further stimulated the area. The first book on metallomics and metalloproteomics was subsequently published by the Royal Society of Chemistry.³ In fact, quantification, speciation and biodistribution of metals (and metalloids) by nuclear analytical techniques have long been initiated in China.⁴ In this themed issue “Metallomics in China”, 19 papers (2 critical reviews, 15 full papers and 2 communications) are published. The collection of the theme roughly reflects the diversity of metallomics research in China.

In view of the potential importance of metal-based nanomaterials in medicine, metallomics of metallo-nanomaterials was reviewed (DOI: 10.1039/c3mt00093a) and in particular the technical aspects of monitoring nano-safety were emphasized. Arsenic widely distributed on earth, is mostly found in minerals together with sulfurs and metals. The latest information on the association of arsenic with macro-and micronutrients in rice plants, was summarized (DOI: 10.1039/c3mt20277a). New information on the mechanism of metallo-anticancer and anti-diabetic agents such as arsenic trioxide and ruthenium(II) complexes, was reported (DOI: 10.1039/c3mt20272k, 10.1039/c3mt20270d). Vanadium complexes were found to be a novel modulator of proliferator-activated receptors (PPAR) (DOI: 10.1039/c3mt20249f), importantly they may play a role in the prevention and treatment of both diabetes and cancer (DOI: 10.1039/c3mt00001j). Selenoproteins were shown to play a role in regulation of redox balance as well as metal homeostasis (DOI: 10.1039/c3mt20282h). The role of metal ions on protein folding and aggregation, inhibition of chaperone activity and protein–protein interactions was reported (DOI: 10.1039/c3mt20262c, 10.1039/c3mt20265h and 10.1039/c3mt00014a), providing useful data on the importance of metals in biology and medicine. The affinity of three submetallomes towards metallothionein (MT2) was examined and rationalized (DOI: 10.1039/c3mt00016h). Although both Zn(II) and Cu(II) bind phosphodiesterase from T. stejnegeri venom, only Cu(II) serves as a switch for the activity of the enzyme (DOI: 10.1039/c3mt00031a). Myoglobins as a protein scaffold was used to study manganese reconstituted-protein in oxidation of hydrogen peroxide and the effect of distal histidine on the catalysis was elaborated (DOI: 10.1039/c3mt20275e).

Nuclear analytical techniques continue to be crucial for metallomics. Synchrotron radiation X-ray fluorescence and X-ray absorption spectroscopy have been used to analyze speciation of mercury, selenium and their relationships (DOI: 10.1039/c3mt20279h, 10.1039/c3mt20273a). Two-dimensional separation system coupled with ICP-MS allows mercury-binding proteins in blood plasma to be characterized more precisely (DOI: 10.1039/c3mt00036b), improving our understanding of the metabolism of the metal in the human body. Novel phosphorescent Ru(III) bipyridine D-fructose complexes allow cellular uptake of the complexes to be tracked readily, so offering a way to develop new agents that exhibit photoinduced cytotoxicity (DOI: 10.1039/c3mt20276c). A metalloproteomic approach can be readily used to track cobalt- and nickel-binding proteins and metal-binding motifs in S. pneumonia (DOI: 10.1039/c3mt00126a). A structural-oriented bioinformatics approach allows spatially histidine-rich clusters to be explored, which can be extended to other single amino acid-rich clusters (DOI: 10.1039/c3mt00026e).

I anticipate that Chinese colleagues will continue to play an increasingly important role in metallomics (and metalloproteomics) research so advancing the inter-disciplinary nature of metallomics among the (bio)chemistry, environmental science, molecular biology, toxicology and medical communities.

Professor Hongzhe Sun, The University of Hong Kong, HK, China.

Editorial Board member, Metallomics.

References

1. G. B. Jiang and B. He, Sci. Found. China, 2005, 19, 151–155.
2. H. Sun and Z. Chai, Annu. Rep. Prog. Chem., Sect. A: Inorg. Chem., 2010, 106, 20–38.
3. C. Chen, Z. Chai and Y. Gao, Nuclear Analytical Techniques for Metallomics and Metalloproteomics, Royal Society of Chemistry, Cambridge, United Kingdom, 2010.
4. Z. Chai, J. Sun and S. Ma, Neutron Activation Analysis in Environmental Sciences, Biological and Geological Sciences, Atomic Energy Press, Beijing, 1992.

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