Back to Search
Start Over
Thiol/Disulfide Redox Switches in the Regulation of Heme Binding to Proteins
- Source :
- Antioxidants & Redox Signaling. 14:1039-1047
- Publication Year :
- 2011
- Publisher :
- Mary Ann Liebert Inc, 2011.
-
Abstract
- This review focuses on thiol/disulfide redox switches that regulate heme binding to proteins and modulate their activities. The importance of redox switches in metabolic regulation and the general mechanism by which redox switches modulate activity are discussed. Methods are described to characterize heme-binding sites and to assess their physiological relevance. For thiol/disulfide interconversion to regulate activity of a system, the redox process must be reversible at the ambient redox potentials found within the cell; thus, methods (and their limitations) are discussed that can address the physiological relevance of a redox switch. We review recent results that define a mechanism for how thiol/disulfide redox switches that control heme binding can regulate the activities of an enzyme, heme oxygenase-2, and an ion channel, the BK potassium channel. The redox switches on these proteins are composed of different types of Cys-containing motifs that have opposite effects on heme affinity, yet have complementary effects on hypoxia sensing. Finally, a model is proposed to describe how the redox switches on heme oxygenase-2 and the BK channel form an interconnected system that is poised to sense oxygen levels in the bloodstream and to elicit the hypoxic response when oxygen levels drop below a threshold value. Antioxid. Redox Signal. 14, 1039–1047.
- Subjects :
- BK channel
Heme binding
Physiology
Clinical Biochemistry
Heme
Plasma protein binding
Models, Biological
Biochemistry
Redox
chemistry.chemical_compound
Disulfides
Molecular Biology
Ion channel
General Environmental Science
chemistry.chemical_classification
biology
Proteins
Cell Biology
Forum Review Articles
Non-innocent ligand
chemistry
biology.protein
Thiol
General Earth and Planetary Sciences
Oxidation-Reduction
Protein Binding
Subjects
Details
- ISSN :
- 15577716 and 15230864
- Volume :
- 14
- Database :
- OpenAIRE
- Journal :
- Antioxidants & Redox Signaling
- Accession number :
- edsair.doi.dedup.....6b06bd354156b4e60fdb2a81fd03ff0c