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Chloride bound to oxidized cytochrome c oxidase controls the reaction with nitric oxide (Articolo in rivista)
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- Chloride bound to oxidized cytochrome c oxidase controls the reaction with nitric oxide (Articolo in rivista) (literal)
- Anno
- 1998-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1074/jbc.273.49.32475 (literal)
- Alternative label
Giuffrè A, Stubauer G, Brunori M, Sarti P, Torres J, Wilson MT (1998)
Chloride bound to oxidized cytochrome c oxidase controls the reaction with nitric oxide
in The Journal of biological chemistry (Print)
(literal)
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- Giuffrè A, Stubauer G, Brunori M, Sarti P, Torres J, Wilson MT (literal)
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- cited By (since 1996)33 (literal)
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- Department of Biochemical Sciences, CNR Center of Molecular Biology, University of Rome La Sapienza, I-00185 Rome, Italy; Department of Biological Sciences, University of Essex, Colchester CO4 3SQ, United Kingdom. (literal)
- Titolo
- Chloride bound to oxidized cytochrome c oxidase controls the reaction with nitric oxide (literal)
- Abstract
- The reaction of nitric oxide (NO) with oxidized fast cytochrome c oxidase was investigated by stopped-flow, amperometry, and EPR, using the enzyme as prepared or after 'pulsing'. A rapid reduction of cytochrome a is observed with the pulsed, but not with the enzyme as prepared. The reactive species (?(max) = 424 nm) reacts with NO at k = 2.2 x 105 M-1 s-1 at 20 °C and is stable for hours unless Cl- is added, in which case it decays slowly (t( 1/2 ) ~ 70 min) to an unreactive state (?(max) = 423 nm) similar to the enzyme as prepared. Thus, Cl- binding prevents a rapid reaction of NO with the oxidized binuclear center. EPR experiments show no new signals within 15 s after addition of NO to the enzyme as prepared. Amperometric measurements show that the pulsed NO-reactive enzyme reacts with high affinity and a stoichiometry of 1 NO/aa3, whereas the enzyme as prepared reacts to a very small extent (<20%). In both cases, the reactivity is abolished by pre-incubation with cyanide. These experiments suggest that the effect of 'pulsing' the enzyme, which leads to enhanced NO reactivity, arises from removing Cl- bound at the oxidized cytochrome a3-Cu(B) site. (literal)
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