Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/77234
Citations
Scopus Web of Science® Altmetric
?
?
Type: Journal article
Title: The Metallothionein/Thionein System: an oxidoreductive metabolic zinc link
Author: Bell, S.
Vallee, B.
Citation: ChemBioChem: a European journal of chemical biology, 2009; 10(1):55-62
Publisher: Wiley-VCH Verlag GMBH
Issue Date: 2009
ISSN: 1439-4227
1439-7633
Statement of
Responsibility: 
Stephen G. Bell and Bert L. Vallee
Abstract: 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 zinc[BOND]thiolate 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.
Keywords: copper
cysteine
metallothionein
oxidoreduction
zinc
Rights: © 2009 Wiley-VCH Verlag GmbH& Co. KGaA, Weinheim
DOI: 10.1002/cbic.200800511
Published version: http://dx.doi.org/10.1002/cbic.200800511
Appears in Collections:Aurora harvest 4
Chemistry and Physics publications

Files in This Item:
There are no files associated with this item.


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.