| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10795903 | Biochimica et Biophysica Acta (BBA) - Bioenergetics | 2012 | 10 Pages |
Abstract
⺠Nitric oxide reacts with the metals of the binuclear site of cytochrome c oxidase which is inhibited. ⺠A nitrosyl-derivative (CcOX-NO) or a nitrite-derivative (CcOX-NO2â) can be formed. ⺠Persistence of inhibition depends on the prevailing mechanism of reaction. ⺠Substrates availability, O2 and cytochrome c2+, and the NO concentration control the mechanism. ⺠Inhibition is O2-competitive only if CcOX nitrosylation occurs.
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Authors
Paolo Sarti, Elena Forte, Daniela Mastronicola, Alessandro Giuffrè, Marzia Arese,