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Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
Published on: December 4, 2017
Iron-based redox switches in biology
F Wayne Outten1, Elizabeth C Theil
1Department of Chemistry and Biochemistry, The University of South Carolina, 631 Sumter Street, Columbia, South Carolina 29208, USA. wayne.outten@chem.sc.edu
Antioxidants & Redox Signaling
|November 22, 2008
Summary
Iron is a vital cofactor in biological processes and acts as a cellular redox sensor. This review covers iron-based redox sensor proteins, including those with iron-sulfur clusters, heme, and other iron sites.
Area of Science:
- Biochemistry
- Molecular Biology
- Cellular Biology
Background:
- Iron is a crucial redox-active cofactor in numerous biological processes like respiration and photosynthesis.
- Iron also functions as a sensor for cellular redox status, regulating protein activity.
- Iron-based sensors utilize Fe-S clusters, heme, and mononuclear iron sites to modulate cellular redox balance.
Purpose of the Study:
- To provide an overview of characterized iron-based redox sensor proteins.
- To highlight the role of iron-sulfur clusters in redox sensing.
- To discuss proteins employing heme or novel iron sites for redox sensing.
Main Methods:
- Biochemical characterization of iron-based redox sensor proteins.
- Review of existing literature on prokaryotic and eukaryotic iron-containing sensor proteins.
Main Results:
- Iron-based sensors, including Fe-S clusters, heme, and mononuclear sites, act as switches controlling protein activity.
- These sensors are found in both prokaryotes and eukaryotes.
- The review emphasizes Fe-S cluster-containing sensors but also includes others.
Conclusions:
- Iron's unique electrochemical properties make it essential for biological redox sensing.
- Iron-based redox sensors are critical for maintaining cellular redox homeostasis.
- Further research into diverse iron-containing redox sensors is warranted.
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