期刊
FREE RADICAL BIOLOGY AND MEDICINE
卷 127, 期 -, 页码 228-237出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.freeradbiomed.2018.03.035
关键词
Selenocysteine; Cysteine; Reversible; Oxidation; Resistance to oxidation; [NiFeSe]-hydrogenase; Glutathione peroxidase; Thioredoxin reductase
资金
- National Institutes of Health [GM069696]
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM069696] Funding Source: NIH RePORTER
This review highlights the contributions of Jean Chaudiere to the field of selenium biochemistry. Chaudiere was the first to recognize that one of the main reasons that selenium in the form of selenocysteine is used in proteins is due to the fact that it strongly resists permanent oxidation. The foundations for this important concept was laid down by Al Tappel in the 1960's and even before by others. The concept of oxygen tolerance first recognized in the study of glutathione peroxidase was further advanced and refined by those studying [NiFeSe]-hydrogenases, selenosubtilisin, and thioredoxin reductase. After 200 years of selenium research, work by Marcus Conrad and coworkers studying glutathione peroxidase-4 has provided definitive evidence for Chaudiere's original hypothesis (Ingold et al., 2018) [36]. While the reaction of selenium with oxygen is readily reversible, there are many other examples of this phenomenon of reversibility. Many reactions of selenium can be described as easy in - easy out. This is due to the strong nucleophilic character of selenium to attack electrophiles, but then this reaction can be reversed due to the strong electrophilic character of selenium and the weakness of the selenium-carbon bond. Several examples of this are described.
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