title: Substrate binding and enzyme function investigated by infrared spectroscopy.
abstract: Protein conformational changes triggered by molecule binding are increasingly investigated by infrared spectroscopy often using caged compounds. Several examples of molecule-protein recognition studies are given, which focus on nucleotide binding to proteins. The investigation of enzyme mechanisms is illustrated in detail using the Ca(2+)-ATPase of the sarcoplasmic reticulum membrane as an example. It is shown that infrared spectroscopy provides valuable information on general aspects of enzyme function as well as on molecular details of molecule-protein interactions and the mechanism of catalysis.
authors.affiliation: Institut für Biophysik, Johann Wolfgang Goethe-Universität, Theodor-Stern-Kai 7, Haus 74, D-60590, Frankfurt am Main, Germany. barth@biophysik.uni-frankfurt.de
authors.forename: A
authors.initials: A
authors.lastname: Barth
authors.forename: C
authors.initials: C
authors.lastname: Zscherp
mesh_terms: D000252:Calcium-Transporting ATPases / Q000378:metabolism*; D012519:Sarcoplasmic Reticulum / Q000201:enzymology; D013055:Spectrophotometry, Infrared; D013379:Substrate Specificity
chemical_list: D000252:Calcium-Transporting ATPases