Abstract
The heme protein wheat germ peroxidase (isoenzyme C2) and its cyanide-inhibited form have been investigated by means of electronic, CD and paramagnetic NMR spectroscopy. The data indicate a protein environment of the active site distinct from that of horseradish peroxidase (HRP), with a larger solvent accessibility. The iron is pentacoordinated at neutral and low pH, whereas a hydroxyl anion may be bound at alkaline pH. The fifth axial ligand is a His residue with a partial anionic character, as found in other peroxidases. A spin equilibrium is observed at high enzyme concentrations.
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Received: 17 September 1996 / Accepted: 10 January 1997
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Fernández, C., Podestá, O., Converso, D. et al. A biophysical characterization of the iron coordination environment in wheat germ peroxidase. JBIC 2, 218–224 (1997). https://doi.org/10.1007/s007750050127
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DOI: https://doi.org/10.1007/s007750050127