Heavy metal derivatives of membrane proteins: selective mercurilation of bacteriorhodopsin
Related Experiment Video
Updated: Oct 24, 2026

A Study of the Complexation of Mercury(II) with Dicysteinyl Tetrapeptides by Electrospray Ionization Mass Spectrometry
Published on: January 8, 2016
H Sigrist1, E Kislig, M Rottenberg
1Institute of Biochemistry, University of Berne, Switzerland.
Abstract:
A method is described for the selective introduction of heavy atoms into structured membrane proteins by a two step modification. The procedure is applied for the purple membrane protein bacteriorhodopsin. Selective heavy-atom modification of this protein is achieved by placing a mercury reagent of intermediate polarity into phenylthiocarbamoylated bacteriorhodopsin. Incorporation of mercury requires the selective phenylthiocarbamoylation of a lysine residue. Optical investigations including circular dichroism document unchanged chromophore-protein and protein-protein interactions in mercury labeled purple membranes.
Related Concept Videos
Oxymercuration-Reduction of Alkenes
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.
Channel Rhodopsins
Rhodopsins belong to the family of cell surface proteins called G-protein coupled receptors,...
Multi-pass Transmembrane Proteins and β-barrels
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as G-protein-linked receptors (GPCRs) and...
Biosynthesis of Lipids
Antiprotozoal Agents

