Nitric oxide and the respiratory enzyme |
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Authors: | Brunori Maurizio Forte Elena Arese Marzia Mastronicola Daniela Giuffrè Alessandro Sarti Paolo |
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Institution: | Department of Biochemical Sciences and CNR Institute of Molecular Biology and Pathology, University of Rome La Sapienza, I-00185 Rome, Italy. maurizio.brunori@uniroma1.it |
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Abstract: | Available information on the molecular mechanisms by which nitric oxide (NO) controls the activity of the respiratory enzyme (cytochrome-c-oxidase) is reviewed. We report that, depending on absolute electron flux, NO at physiological concentrations reversibly inhibits cytochrome-c-oxidase by two alternative reaction pathways, yielding either a nitrosyl- or a nitrite-heme a3 derivative. We address a number of hypotheses, envisaging physiological and/or pathological effects of the reactions between NO and cytochrome-c-oxidase. |
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