Related Experiment Video
Updated: Jul 7, 2026

Production of Disulfide-stabilized Transmembrane Peptide Complexes for Structural Studies
Published on: March 6, 2013
Proton coupling to [4Fe-4S](2+/+) and [4Fe-4Se](2+/+) oxidation and reduction in a designed protein
Michelle L Kennedy1, Brian R Gibney
1Department of Chemistry, Columbia University, New York, New York 10027, USA.
Abstract:
The coupling of a single proton to [4Fe-4S]2+/+ oxidation/reduction in a de novo designed iron-sulfur protein maquette is presented. The reduced state pKared is 9.3, and the oxidized state pKaox is <6.5. The reduced state pKared shifts to 8.3 upon incorporation of a [4Fe-4Se]2+/+ cluster, implicating the cluster itself or its primary coordination sphere as the proton-coupling site.
Related Concept Videos
Electron Transport Chains
The ETC is comprised of...
The Supercomplexes in the Crista Membrane
Protein Modifications in the RER
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
Electron Transport Chain: Complex III and IV
Protein Denaturation
Electron Transport Chain Components
![Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase](/_next/image?url=https%3A%2F%2Fcloudfront.jove.com%2FCDNSource%2Fteasers%2F55858.jpg&w=3840&q=50)
