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Probing the high-affinity site of beef heart cytochrome c oxidase by cross-linking (Articolo in rivista)
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- Probing the high-affinity site of beef heart cytochrome c oxidase by cross-linking (Articolo in rivista) (literal)
- Anno
- 1996-01-01T00:00:00+01:00 (literal)
- Alternative label
Malatesta F, Antonini G, Nicoletti F, Giuffrè A, D'Itri E, Sarti P, Brunori M (1996)
Probing the high-affinity site of beef heart cytochrome c oxidase by cross-linking
in Biochemical journal (Lond., 1984)
(literal)
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- Malatesta F, Antonini G, Nicoletti F, Giuffrè A, D'Itri E, Sarti P, Brunori M (literal)
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- cited By (since 1996)9 (literal)
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- Dipartimento di Biologia di Base ed Applicata, Universita' di L'Aquila, L'Aquila, Italy; Dipartimento di Scienze Biochimiche, Centro di Biologia Molecolare del CNR, Universita' di Roma 'La Sapienza', Roma, Italy; Istituto di Chimica Biologica, Universita' di Cagliari, Cagliari, Italy (literal)
- Titolo
- Probing the high-affinity site of beef heart cytochrome c oxidase by cross-linking (literal)
- Abstract
- A covalent complex between cytochrome c oxidase and Saccharomyces cerevisiae iso-1-cytochrome c (called caa3) has been prepared at low ionic strength. Subunit III Cys-115 of beef heart cytochrome c oxidase cross-links by disulphide bond formation to thionitrobenzoate-modified yeast cytochrome c, a derivative shown to bind into the high-affinity site for substrate. Stopped-flow experiments show that (1) covalently bound yeast cytochrome c cannot donate electrons to cytochrome oxidase, whereas oxidation of exogenously added cytochrome c and electron transfer to cytochrome a are only slightly affected; (2) the steady-state reduction levels of cytochrome c and cytochrome ? in the covalent complex caa3 are higher than those found in the native aa3 enzyme. However, (3) K(m) and V(max) values obtained from the non-linear Eadie-Hofstee plots are very similar in both caa3 and aa3. The results imply that cytochrome c bound to the high-affinity site is not in a configuration optimal for electron transfer. (literal)
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