Telluromethionine

Telluromethionine (sometimes shortened to TeMet) is a rare and natural <a href="/facts/Amino_acid/WDxYwBny">amino acid</a>. It is a heavy analog of <a href="/facts/Methionine/7neydPKo">methionine</a> and <a href="/facts/Selenomethionine/WjFvYRxf">selenomethionine</a> containing <a href="/facts/Tellurium/v7QvfIvS">tellurium</a>. Telluromethionine has been suggested as a probe for structural biochemistry, as it can be incorporated into <a href="/facts/Protein/Jxmagu3E">proteins</a> and used for <a href="/facts/X-ray_crystallography/WtI0F5DN">X-ray crystallography</a> and <a href="/facts/Nuclear_magnetic_resonance_spectroscopy/SFKgdthI">NMR</a> measurements.
In aqueous solutions, telluromethioning oxidizes to a <a href="/facts/Telluroxide/BwIDGD2e">telluroxide</a>, but can be recovered by use of <a href="/facts/Dithiothreitol/sUFKRIAg">DTT</a>. Telluromethionine is not very stable in wheat germ extract, which impacts its <a href="/facts/Translation_(biology)/JcPC1rth">translation</a> rate. In the extract, elemental tellurium seems to form, suggesting a degradation mechanism, but this is not well understood. However, enriching proteins with tellurium in <a href="/facts/Auxotrophy/N0gVSzJV">auxotrophic</a> <a href="/facts/E._coli/nR4Gvl56">E. coli</a> was successfully used to express several <a href="/facts/Recombinant_proteins/dT3PL7M6">recombinant</a> proteins.

Telluromethionine open-in-new

Telluromethionine