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Modulation of O-2 reduction in Saccharomyces cerevisiae mitochondria
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Number of Authors: 22017 (English)In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 591, no 24, p. 4049-4055Article in journal (Refereed) Published
Abstract [en]

Respiratory supercomplex factor (Rcf) 1 is a membrane-bound protein that modulates the activity of cytochrome c oxidase (CytcO) in Saccharomycescerevisiae mitochondria. To investigate this regulatory mechanism, we studied the interactions of CytcO with potassium cyanide (KCN) upon removal of Rcf Delta. While the addition of KCN to the wild-type mitochondria results in a full reduction of heme a, with the rcf Delta mitochondria, a significant fraction remains oxidized. Upon addition of ascorbate in the presence of O-2 and KCN, the reduction level of hemes a and b was a factor of similar to 2 larger with the wild-type than with the rcf Delta mitochondria. These data indicate that turnover of CytcO was less blocked in rcf Delta than in the wild-type mitochondria, suggesting that Rcf Delta modulates the structure of the catalytic site.

Place, publisher, year, edition, pages
2017. Vol. 591, no 24, p. 4049-4055
Keywords [en]
cytochrome aa(3), cytochrome c oxidase, electron transfer, membrane protein, respiratory supercomplex factor, Saccharomy cescerevisiae
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:su:diva-152520DOI: 10.1002/1873-3468.12918ISI: 000418825700008PubMedID: 29171870OAI: oai:DiVA.org:su-152520DiVA, id: diva2:1180474
Available from: 2018-02-05 Created: 2018-02-05 Last updated: 2018-02-05Bibliographically approved

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