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Preparation and Reactions of Thiols

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Directly Acting Muscle Relaxants: Dantrolene and Botulinum Toxin

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Related Experiment Video

Updated: Jul 15, 2026

Genetic and Biochemical Approaches for In Vivo and In Vitro Assessment of Protein Oligomerization: The Ryanodine Receptor Case Study

Genetic and Biochemical Approaches for In Vivo and In Vitro Assessment of Protein Oligomerization: The Ryanodine Receptor Case Study

Published on: July 27, 2016

Non-thiol reagents regulate ryanodine receptor function by redox interactions that modify reactive thiols.

Benjamin S Marinov¹, Rotimi O Olojo, Ruohong Xia

¹Physics Department, Portland State University, Portland, Oregon 97207, USA.

Antioxidants & Redox Signaling

|May 1, 2007

Summary

Channel activators and inhibitors interact with the Ca(2+) release channel (CRC) by acting as electron acceptors or donors, influencing thiol redox states. This electron exchange mechanism modulates CRC activity.

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Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella

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Last Updated: Jul 15, 2026

Genetic and Biochemical Approaches for In Vivo and In Vitro Assessment of Protein Oligomerization: The Ryanodine Receptor Case Study

Genetic and Biochemical Approaches for In Vivo and In Vitro Assessment of Protein Oligomerization: The Ryanodine Receptor Case Study

Published on: July 27, 2016

Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella

Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella

Published on: November 30, 2018

Area of Science:

Biochemistry
Molecular Biology
Physiology

Background:

The Ca(2+) release channel (CRC) in the sarcoplasmic reticulum (SR) is crucial for muscle contraction.
CRC activity is modulated by thiol group oxidation/reduction, but the mechanism of non-thiol regulators is unclear.

Purpose of the Study:

To elucidate the mechanism by which non-thiol regulators modulate CRC activity.
To investigate the role of electron transfer in CRC regulation.

Main Methods:

Studied the interaction of channel activators and inhibitors with CRC.
Analyzed the redox properties of thiol groups on the ryanodine receptor (RyR).
Investigated competitive interactions between known activators and inhibitors.

Main Results:

Identified channel activators as electron acceptors and inhibitors as electron donors in free radical reactions.
Demonstrated competitive binding between caffeine (activator) and tetracaine (inhibitor).
Showed that activators shift thiol redox potential to more negative values, while inhibitors shift it to more positive values.

Conclusions:

Non-thiol channel modulators regulate CRC by transiently exchanging electrons with the protein.
This electron exchange influences the thiol-disulfide balance within the CRC.
A common binding site likely integrates the donor/acceptor effects of various ligands.