Redox signaling: thiol chemistry defines which reactive oxygen and nitrogen species can act as second messengers.

Abstract

Except for the role of NO in the activation of guanylate cyclase, which is well established, the involvement of reactive oxygen species (ROS) and reactive nitrogen species (RNS) in signal transduction remains controversial, despite a large body of evidence suggestive of their participation in a variety of signaling pathways. Several problems have limited their acceptance as signaling molecules, with the major one being the difficulty in identifying the specific targets for each pathway and the chemical reactions supporting reversible oxidation of these signaling components, consistent with a second messenger role for ROS and RNS. Nevertheless, it has become clear that cysteine residues in the thiolate (i.e., ionized) form that are found in some proteins can be specific targets for reaction with H(2)O(2) and RNS. This review focuses on the chemistry of the reversible oxidation of those thiolates, with a particular emphasis on the critical thiolate found in protein tyrosine phosphatases as an example.

3 Figures and Tables

050100150'05'06'07'08'09'10'11'12'13'14'15'16'17
Citations per Year

1,301 Citations

Semantic Scholar estimates that this publication has 1,301 citations based on the available data.

See our FAQ for additional information.

Cite this paper

@article{Forman2004RedoxST, title={Redox signaling: thiol chemistry defines which reactive oxygen and nitrogen species can act as second messengers.}, author={Henry Jay Forman and Jon M. Fukuto and Martine Torres}, journal={American journal of physiology. Cell physiology}, year={2004}, volume={287 2}, pages={C246-56} }