Characterization by mass spectrometry and IRMPD spectroscopy of the sulfoxide group in oxidized methionine and related compounds
作者:Marta Ignasiak、Debora Scuderi、Pedro de Oliveira、Tomasz Pedzinski、Yamina Rayah、Chantal Houée Levin
DOI:10.1016/j.cplett.2010.12.012
日期:2011.1
Methionine protein residues are prone to oxidation. To unravel the controversy about the mechanism of its one-electron oxidation, we characterised the main biological product, methionine sulfoxide, using mass spectrometry and IR multiple photon dissociation spectroscopy.
bond through hydrogen selenide (H2Se) and hypobromousacid (HOBr), which can be easily controlled at simulated physiological conditions. This novel strategy provides a circulation regulation system to modulate the sulfilimine bond in peptides and NC1 hexamers, which can offer a substantial system for further study of the physiological function of collagen IV.
Slow-binding inhibition of peptide deformylase by cyclic peptidomimetics as revealed by a new spectrophotometric assay
作者:Kiet T. Nguyen、Xubo Hu、Dehua Pei
DOI:10.1016/j.bioorg.2004.01.001
日期:2004.6
UV-Vis spectrophotometer or a fluorimeter in a continuous fashion. The utility of the assay was demonstrated by determining the catalytic activity of PDF and the inhibition constants of PDF inhibitors. These studies revealed the slow-binding behavior of a previously reported macrocyclic PDF inhibitor. This method offers several advantages over the existing PDF assays and should be particularly useful