Optical characteristics of thiamine in model systems and in holoenzyme.
The optical properties of thiamine diphosphate-dependent enzymes change significantly on their interaction with cofactors (thiamine, bivalent metal ions) and substrates. These changes are connected with structural alterations of the active site and the mechanism of its functioning, and in some cases they reflect changes in the optical properties of the coenzyme itself within the protein. The use of optical characteristics, especially together with model systems, appeared to be a rather promising approach for investigation of the active site of thiamine diphosphate-dependent enzymes and the mechanism of its functioning. So, it seemed to be useful to summarize the literature data concerning the optical characteristics of thiamine (thiamine diphosphate) in model systems and the efficiency of their application for study of thiamine diphosphate-dependent enzymes.
Sevostyanova
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IA
Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow, 119992, Russia.
Kochetov
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GA
D002942:Circular Dichroism; D003067:Coenzymes / Q000378:metabolism; D004798:Enzymes / Q000737:chemistry / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008670:Metals / Q000737:chemistry / Q000378:metabolism; D008956:Models, Chemical; D015394:Molecular Structure; D013053:Spectrophotometry; D013835:Thiamine Pyrophosphate / Q000737:chemistry / Q000378:metabolism
D003067:Coenzymes; D004798:Enzymes; D008670:Metals; D013835:Thiamine Pyrophosphate