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  Characterization of a quinole-oxidase activity in crude extracts of Thermoplasma acidophilum and isolation of an 18-kDa cytochrome

Gärtner, P. (1991). Characterization of a quinole-oxidase activity in crude extracts of Thermoplasma acidophilum and isolation of an 18-kDa cytochrome. European Journal of Biochemistry, 200(1), 215-222. doi:10.1111/j.1432-1033.1991.tb21070.x.

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 Creators:
Gärtner, Peter1, Author              
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1Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              

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 Abstract: A quinol-oxidase activity was detected in crude extracts of the thermoacidophilic archaebacterium Thermoplasma acidophilum. The activity was optimal at pH 5.4 and 50°C. The Km for ubiquinol-10 was 18 microM. The enzyme was inhibited by 2n-heptyl-4-hydroxyquinoline N-oxide with a Ki of 150 nM. Ubiquinols with different side-chain lengths were oxidized at similar rates, whereas menaquinols were converted at 6-12-fold higher rates compared to ubiquinols. Membranes from T. acidophilum contain cytochromes of b, d and a1 types, as shown by optical spectroscopy. CO difference spectroscopy suggests the existence of a cytochrome o. A b-type cytochrome with an apparent molecular mass of 18 kDa was purified in the presence of high detergent concentrations. It readily forms dimers on SDS/PAGE. This cytochrome also contains Cu, as shown by atomic-absorption spectroscopy. Redox titration suggests that the 18-kDa cytochrome may contain 2 heme groups; b558 with a midpoint potential of 75 mV and b562/553 with a midpoint potential of -150 mV.

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Language(s): eng - English
 Dates: 1991-03-191991-01-162005-03-031991-08-01
 Publication Status: Published in print
 Pages: 8
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1111/j.1432-1033.1991.tb21070.x
PMID: 1879426
 Degree: -

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Title: European Journal of Biochemistry
Source Genre: Journal
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Publ. Info: Berlin : Published by Springer-Verlag on behalf of the Federation of European Biochemical Societies
Pages: - Volume / Issue: 200 (1) Sequence Number: - Start / End Page: 215 - 222 Identifier: ISSN: 0014-2956
CoNE: https://pure.mpg.de/cone/journals/resource/111097776606040