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Cited by 307

The DOI matches its Crossref record; 11 of the 11 references it cites were found in a registry or an index.

Zinc Coordination Environments in Proteins as Redox Sensors and Signal Transducers

Maret, Wolfgang·2006·Antioxidants & Redox Signaling

Abstract

Zinc/cysteine coordination environments in proteins are redox-active. Oxidation of the sulfur ligands mobilizes zinc, while reduction of the oxidized ligands enhances zinc binding, providing redox control over the availability of zinc ions. Some zinc proteins are redox sensors, in which zinc release is coupled to conformational changes that control varied functions such as enzymatic activity, binding interactions, and molecular chaperone activity. Whereas the released zinc ion in redox sensors has no known function, the redox signal is transduced to specific and sensitive zinc signals in redox transducers. Released zinc can bind to sites on other proteins and modulate signal transduction, generation of metabolic energy, mitochondrial function, and gene expression. The paradigm of such redox transducers is the zinc protein metallothionein, which, together with its apoprotein, thionein, functions at a central node in cellular signaling by redistributing cellular zinc, presiding over the availability of zinc, and interconverting redox and zinc signals. In this regard, the transduction of nitric oxide (NO) signals into zinc signals by metallothionein has received particular attention. It appears that redox-inert zinc has been chosen to control some aspects of cellular thiol/disulfide redox metabolism. Tight control of zinc is essential for redox homeostasis because both increases and decreases of cellular zinc elicit oxidative stress. Depending on its availability, zinc can be cytoprotective as a pro-antioxidant or cytotoxic as a pro-oxidant. Any condition with acute or chronic oxidative stress is expected to perturb zinc homeostasis.

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Crossref · 10.1089/ars.2006.8.1419

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Metadata

Authors
Maret, W.
Venue
Antioxidants & Redox Signaling
Published
2006-09
Volume
8
Issue
9-10
Pages
1419-1441
ISSN
  • 1523-0864 (ISSN-L)
  • 1557-7716
OpenAlex
W2012122987
Cited by
307
References
11
FWCI
17.64
Type
journal article
Language
en
Open access
closed

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