[Role of the electron acceptor properties of lysozyme and its substrate inhibitors in photosensitized electron transport in their complexes by the EPR method]. / Izuchenie roli élektronoaktseptornykh svoistv lizotsima i ego substrat-ingibitorov v fotosensibilizirovannom perenose élektronov v ikh kompleksakh metodom EPR.

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.

[Localization of unpaired electrons in molecules of the substrate inhibitors of lysozyme. II. Oligosaccharides]. / Issledovanie lokalizatsii nesparennykh élektronov v molekulakh substrat-ingibitorov lizotsima. II. Oligosakharidy.

It has been shown by the method of electron photosensitized transfer that N-acetyl group is the main electron-acceptor group in oligomeres of N-acetyl glucose amine (AGA). In n-AGA molecules (n-3.5) interacting with an electron radical products of the breakage of glycoside bond are observed, their concentration rising with an increase of the chain length. The ionic strength does not affect the photosensitized transfer of the electron in chitin oligomeres. Formation of paramagnetic centres in the molecule penta-AGA depends on the medium pH.