Abstract
Electron paramagnetic resonance studies of ferrous nitric oxide complexes of turnip isoperoxidases have shown that the proteic ligand of the heme iron is always a nitrogen atom and that the paramagnetic center symmetry is rhombic. The addition of indoleacetic acid to nitrosyl ferrous peroxidases produced in some cases drastic spectral changes. Indoleacetic acid does not displace nitric oxide, but an interaction does take place between the nitric oxide heme complex and the substrate binding site. Another interaction with a proton binding site is also suggested in the case of horseradish peroxidase.
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