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Substrate binding and enzyme function investigated by infrared spectroscopy
Author(s) -
Barth Andreas,
Zscherp Christian
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01782-8
Subject(s) - chemistry , enzyme , molecule , infrared spectroscopy , function (biology) , substrate (aquarium) , biophysics , force spectroscopy , spectroscopy , endoplasmic reticulum , biochemistry , biology , microbiology and biotechnology , organic chemistry , physics , ecology , quantum mechanics
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.