Horseradish peroxidase monitored by infrared spectroscopy: effect oftemperature, substrate and calcium

Kaposi, András Dezső and Fidy, Judit and Manas, E. S. and Vanderkooi, J. M. and Wright WW, W. W. (1999) Horseradish peroxidase monitored by infrared spectroscopy: effect oftemperature, substrate and calcium. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY, 1435 (1-2). pp. 41-50. ISSN 0167-4838

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Abstract

Horseradish peroxidase was examined as a function of Ca and substrate binding using infrared spectroscopy in the temperature range of 10-300 K. The Ca complex could be identified by the carboxylate stretches. The amide peak positions indicate that the protein remains stable from room temperature to 10 K. Shifts in these peaks are consistent with increased hydrogen bonding as temperature decreases, but the protein conformation is maintained at cryogenic temperatures. The substrate, benzohydroxamic acid, produced no detectable change in the infrared spectrum, consistent with X-ray crystallography results. With removal of Ca, the protein maintained its overall helicity. (C) 1999 Elsevier Science B.V. All rights reserved.

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