http://www.cnr.it/ontology/cnr/individuo/prodotto/ID253116
Cytochrome c oxidase does not catalyze the anaerobic reduction of NO (Articolo in rivista)
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- Cytochrome c oxidase does not catalyze the anaerobic reduction of NO (Articolo in rivista) (literal)
- Anno
- 1998-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1006/bbrc.1998.8457 (literal)
- Alternative label
Stubauer G, Giuffrè A, Brunori M, Sarti P (1998)
Cytochrome c oxidase does not catalyze the anaerobic reduction of NO
in Biochemical and biophysical research communications (Print)
(literal)
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- Stubauer G, Giuffrè A, Brunori M, Sarti P (literal)
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- cited By (since 1996)49 (literal)
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- http://www.scopus.com/inward/record.url?eid=2-s2.0-0032540134&partnerID=40&md5=bd6c57e51f334c88176a2d35c96dd032 (literal)
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- Department of Biochemical Sciences, CNR Center of Molecular Biology, Univ. of Rome La Sapienza, 00185, Rome, Italy (literal)
- Titolo
- Cytochrome c oxidase does not catalyze the anaerobic reduction of NO (literal)
- Abstract
- A possible role of reduced cytochrome c oxidase in the metabolism of nitric oxide (NO) has been examined with amperometric and stopped-flow photometric techniques. Reduced purified cytochrome c oxidase and mitochondria showed no catalytic reaction with NO under anaerobic conditions within more than 30 minutes. Only fast binding of NO to the reduced enzyme in a 1:1 stoichiometric ratio was observed. The NO binding rate was strongly decreased in the presence of 1 mM cyanide. These data indicate that, contrary to previous proposals, cytochrome c oxidase in the absence of oxygen does not contribute to physiological NO metabolism. (literal)
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