Investigation of interaction between methemoglobin and polymethacrylates containing imidazole or hydrophobic side chains by means of epr spectroscopy

Autor:	M. Kühn, J. Štamberg, K. Pommerening, O. Ristau, Milan J. Beneš, P. Mohr
Rok vydání:	2007
Předmět:	Steric effects Cytochrome biology General Engineering Photochemistry Methemoglobin law.invention chemistry.chemical_compound Adsorption chemistry law Polymer chemistry biology.protein Side chain Imidazole Electron paramagnetic resonance Spectroscopy
Zdroj:	Journal of Polymer Science: Polymer Symposia. 68:79-88
ISSN:	1936-0959 0360-8905
DOI:	10.1002/polc.5070680111
Popis:	Macroporous polymethacrylates containing imidazole groups as well as hydrophobic side chains adsorb methemoglobin (metHb). The protein-matrix interaction was investigated by means of an electron paramagnetic resonance (EPR) spectroscopy. The adsorption of metHb to the imidazole containing matrices occurs by complex formation with the iron of the prosthetic group. In case of steric hindrance or long spacers, this complex formation is not primarily responsible for the adsorption. The binding of metHb to hydrophobic side chains clearly demonstrates the presence of a metHb-H2O-metHb-OH mixture. Moreover, the protein-matrix interaction induces conformational changes in the protein component. In this case, additional signals in the EPR spectra indicate the formation of a cytochrome P450-like structure.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::11333b882415b1b53245e966a4e9c574 https://doi.org/10.1002/polc.5070680111 Zobrazit plný text záznamu