http://www.cnr.it/ontology/cnr/individuo/prodotto/ID253057
Sulfolobus acidocaldarius terminal oxidase. A kinetic investigation and its structural interpretation (Articolo in rivista)
- Type
- Label
- Sulfolobus acidocaldarius terminal oxidase. A kinetic investigation and its structural interpretation (Articolo in rivista) (literal)
- Anno
- 1994-01-01T00:00:00+01:00 (literal)
- Alternative label
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- Giuffrè A; Antonini G; Brunori M; D'Itri E; Malatesta F; Nicoletti F; Anemuller S; Gleissner M; Schafer G (literal)
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- cited By (since 1996)11 (literal)
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- http://www.scopus.com/inward/record.url?eid=2-s2.0-0027973073&partnerID=40&md5=afb025188df0aa373eb485d27fc524dc (literal)
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- Department of Biochemical Sciences, Universities of Rome 'La Sapienza' and 'Tor Vergata' and
CNR Center of Molecular Biology, Rome, Italy; Institute of Biochemistry, Medical University of Lubeck,
Lubeck, Germany. (literal)
- Titolo
- Sulfolobus acidocaldarius terminal oxidase. A kinetic investigation and its structural interpretation (literal)
- Abstract
- The thermoacidophilic archaebacterium Sulfolobus acidocaldarius possesses a very unusual terminal oxidase. We report original kinetic experiments on membranes of this microorganism carried out by stopped flow, using time- resolved optical spectroscopy combined with singular value decomposition analysis. The reduced-oxidized kinetic difference spectrum of the Sulfolobus membranes is characterized by three significant peaks in the visible region at 605, 586, and 560 nm. The 605-nm peak and part of the 586-nm peak (cytochrome aa3-type quinol oxidase) are reduced synchronously by both ascorbate plus N,N,N',N'-tetramethyl-p-phenylen-diamine (TMPD) and dithionite, and they are very rapidly oxidized by molecular oxygen. A second pool of cytochromes seems to contribute to the 586-nm peak which is not reduced by ascorbate plus TMPD and reacts very slowly with dithionite. The b- type cytochromes (560 nm peak) are reduced by both reductants and are essentially 'non-autoxidizable' at room temperature. Only one CO binding site with spectral features, kinetic properties, and ligand affinity not very dissimilar from those of mammalian cytochrome oxidase can be detected in the ascorbate-reduced membranes. On the contrary, a second CO binding site having unusual properties for aa3 terminal oxidases can be detected in the dithionite-reduced membranes. (literal)
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