Role of the electron acceptor properties of lysozyme and its substrate inhibitors in photosensitized electron transport in their complexes by the EPR method
Kuropteva, Z.V.; Avdeeva, O.S.; Pulatova, M.K.; Kravchenko, N.A.
Biofizika 23(4): 576-582
1978
ISSN/ISBN: 0006-3029 PMID: 28153 Document Number: 138018
The nature of electron-acceptor groups in the system of lysozyme with its substrate-inhibitors has been studied in a wide range of pH values by the method of photosensitized electron transfer. In the lysozyme molecule disulphide bonds and peptide groups are the electron--acceptor groups. The nature of radicals in irradiated lysozyme depends on pH. At complex-formation of lysozyme with oligomeres of N-acetylglucosamine the electron transfer from the enzyme molecule to N-acetyl group of the substrate-inhibitor molecule is realized. Under conditions ruling out complex-formation of lysozyme with the inhibitors (N-acetylglucosamine and its dimer) the electrons are localized on disulphide bonds of the protein molecules at alkaline pH and at pH less than or equal to 3 the radicals are observed which are due to the remove of hydrogen atom from the Calpha-atom of the protein polypeptide chain.