Review
doi: 10.1089/ars.2006.8.835.
Zinc center as redox switch--new function for an old motif
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- PMID: 16771674
- DOI: 10.1089/ars.2006.8.835
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Review
Zinc center as redox switch--new function for an old motif
Antioxid Redox Signal.
2006 May-Jun.
Free article
Abstract
Oxidative stress affects a wide variety of different cellular processes. Now, an increasing number of proteins have been identified that use the presence of reactive oxygen species or alterations in the cellular thiol-disulfide state as regulators of their protein function. This review focuses on two members of this growing group of redox-regulated proteins that utilize a cysteine-containing zinc center as the redox switch: Hsp33, the first molecular chaperone, whose ability to protect cells against stress-induced protein unfolding depends on the presence of reactive oxygen species and RsrA, the first anti-sigma factor that uses a cysteine-containing zinc center to sense and respond to cellular disulfide stress.
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