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The Metallothionein/Thionein System: An Oxidoreductive Metabolic Zinc Link
Author(s) -
Bell Stephen G.,
Vallee Bert L.
Publication year - 2009
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200800511
Subject(s) - metallothionein , zinc , chemistry , biochemistry , organism , redox , metabolism , metalloprotein , oxidative stress , plasma protein binding , biophysics , microbiology and biotechnology , biology , enzyme , genetics , inorganic chemistry , organic chemistry
Metallothioneins (MTs) were discovered more than 50 years ago and identified as low‐molecular weight, sulfhydryl‐rich proteins that were subsequently found to bind zinc predominantly. The binding of seemingly redox inactive zinc ions allows MT to play a central role in oxidoreductive cellular metabolism, cellular zinc distribution and homeostasis. In this interpretive study, we discuss the interaction of MT with physiologically relevant molecules and its effect on zincthiolate bonds. These interactions are linked to recent progress in the functional role of MT in cellular zinc transport, energy production, and protection of the organism against oxidative stress and neurodegenerative diseases.