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Yeast Sco1, a Protein Essential for Cytochrome cOxidase Function Is a Cu(I)-binding Protein

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Nittis, Thalia, George, Graham N., Winge, Dennis R.·2001·Journal of Biological Chemistry

Abstract

Sco1 is a conserved essential protein, which has been implicated in the delivery of copper to cytochrome c oxidase, the last enzyme of the electron transport chain. In this study, we show for the first time that the purified C-terminal domain of yeast Sco1 binds one Cu(I)/monomer. X-ray absorption spectroscopy suggests that the Cu(I) is ligated via three ligands, and we show that two cysteines, present in a conserved motif CXXXC, and a conserved histidine are involved in Cu(I) ligation. The mutation of any one of the conserved residues in Sco1 expressed in yeast abrogates the function of Sco1 resulting in a non-functional cytochrome c oxidase complex. Thus, the function of Sco1 correlates with Cu(I) binding. Data obtained from size-exclusion chromatography experiments with mitochondrial lysates suggest that full-length Sco1 may be oligomeric in vivo.

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Metadata

Authors
Nittis, T., George, G. N., & Winge, D. R.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2001-11
Volume
276
Issue
45
Pages
42520-42526
ISSN
0021-9258 (ISSN-L)
OpenAlex
W2087813537
Cited by
183
References
0
FWCI
4.67
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Yeast Sco1, a Protein Essential for Cytochrome cOxidase Function Is a Cu(I)-binding Protein. https://app.cochat.ai/papers/10.1074/jbc.m107077200
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Nittis, T., George, G. N., & Winge, D. R. (2001). Yeast Sco1, a Protein Essential for Cytochrome cOxidase Function Is a Cu(I)-binding Protein. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m107077200

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.