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Human Sco1 functional studies and pathological implications of the P174L mutant

The pathogenic mutant (P174L) of human Sco1 produces respiratory chain deficiency associated with cytochrome c oxidase (CcO) assembly defects. The solution structure of the mutant in its Cu(I) form shows that Leu-174 prevents the formation of a well packed hydrophobic region around the metal-binding... Full description

Journal Title: Proceedings of the National Academy of Sciences of the United States of America Jan 2, 2007, Vol.104(1), p.15
Main Author: Banci, Lucia
Other Authors: Bertini, Ivano , Ciofi-Baffoni, Simone , Leontari, Iliana
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: ISSN: 00278424 ; E-ISSN: 10916490
Link: http://search.proquest.com/docview/201320543/?pq-origsite=primo
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title: Human Sco1 functional studies and pathological implications of the P174L mutant
format: Article
creator:
  • Banci, Lucia
  • Bertini, Ivano
  • Ciofi-Baffoni, Simone
  • Leontari, Iliana
subjects:
  • Enzymes
  • Nuclear Magnetic Resonance–NMR
  • Mass Spectrometry
  • Copper
  • Biochemistry
ispartof: Proceedings of the National Academy of Sciences of the United States of America, Jan 2, 2007, Vol.104(1), p.15
description: The pathogenic mutant (P174L) of human Sco1 produces respiratory chain deficiency associated with cytochrome c oxidase (CcO) assembly defects. The solution structure of the mutant in its Cu(I) form shows that Leu-174 prevents the formation of a well packed hydrophobic region around the metal-binding site and causes a reduction of the affinity of copper(I) for the protein. K... values for Cu(I)WT-HSco1 and Cu(I)P174L-HSco1 are ... and ..., respectively. The reduction potentials of the two apo proteins are similar, but slower reduction/oxidation rates are found for the mutant with respect to the WT. The mitochondrial metallochaperone in the partially oxidize ... form, at variance with the fully reduced Cu...(I)Coxl7, interacts transiently with both WT-HSco1 and the mutant, forming the Coxl7/Cu(I)/HSco1 complex, but copper is efficiently transferred only in the case of WT protein. ... indeed has an affinity for copper(I) (...) higher than that of the P174L-HSco1 mutant but lower than that...
language: eng
source:
identifier: ISSN: 00278424 ; E-ISSN: 10916490
fulltext: fulltext
issn:
  • 00278424
  • 0027-8424
  • 10916490
  • 1091-6490
url: Link


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titleHuman Sco1 functional studies and pathological implications of the P174L mutant
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ispartofProceedings of the National Academy of Sciences of the United States of America, Jan 2, 2007, Vol.104(1), p.15
identifierISSN: 00278424 ; E-ISSN: 10916490
subjectEnzymes ; Nuclear Magnetic Resonance–NMR ; Mass Spectrometry ; Copper ; Biochemistry
descriptionThe pathogenic mutant (P174L) of human Sco1 produces respiratory chain deficiency associated with cytochrome c oxidase (CcO) assembly defects. The solution structure of the mutant in its Cu(I) form shows that Leu-174 prevents the formation of a well packed hydrophobic region around the metal-binding site and causes a reduction of the affinity of copper(I) for the protein. K... values for Cu(I)WT-HSco1 and Cu(I)P174L-HSco1 are ... and ..., respectively. The reduction potentials of the two apo proteins are similar, but slower reduction/oxidation rates are found for the mutant with respect to the WT. The mitochondrial metallochaperone in the partially oxidize ... form, at variance with the fully reduced Cu...(I)Coxl7, interacts transiently with both WT-HSco1 and the mutant, forming the Coxl7/Cu(I)/HSco1 complex, but copper is efficiently transferred only in the case of WT protein. ... indeed has an affinity for copper(I) (...) higher than that of the P174L-HSco1 mutant but lower than that...
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titleHuman Sco1 functional studies and pathological implications of the P174L mutant
descriptionThe pathogenic mutant (P174L) of human Sco1 produces respiratory chain deficiency associated with cytochrome c oxidase (CcO) assembly defects. The solution structure of the mutant in its Cu(I) form shows that Leu-174 prevents the formation of a well packed hydrophobic region around the metal-binding site and causes a reduction of the affinity of copper(I) for the protein. K... values for Cu(I)WT-HSco1 and Cu(I)P174L-HSco1 are ... and ..., respectively. The reduction potentials of the two apo proteins are similar, but slower reduction/oxidation rates are found for the mutant with respect to the WT. The mitochondrial metallochaperone in the partially oxidize ... form, at variance with the fully reduced Cu...(I)Coxl7, interacts transiently with both WT-HSco1 and the mutant, forming the Coxl7/Cu(I)/HSco1 complex, but copper is efficiently transferred only in the case of WT protein. ... indeed has an affinity for copper(I) (...) higher than that of the P174L-HSco1 mutant but lower than that...
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titleHuman Sco1 functional studies and pathological implications of the P174L mutant
authorBanci, Lucia ; Bertini, Ivano ; Ciofi-Baffoni, Simone ; Leontari, Iliana
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abstractThe pathogenic mutant (P174L) of human Sco1 produces respiratory chain deficiency associated with cytochrome c oxidase (CcO) assembly defects. The solution structure of the mutant in its Cu(I) form shows that Leu-174 prevents the formation of a well packed hydrophobic region around the metal-binding site and causes a reduction of the affinity of copper(I) for the protein. K... values for Cu(I)WT-HSco1 and Cu(I)P174L-HSco1 are ... and ..., respectively. The reduction potentials of the two apo proteins are similar, but slower reduction/oxidation rates are found for the mutant with respect to the WT. The mitochondrial metallochaperone in the partially oxidize ... form, at variance with the fully reduced Cu...(I)Coxl7, interacts transiently with both WT-HSco1 and the mutant, forming the Coxl7/Cu(I)/HSco1 complex, but copper is efficiently transferred only in the case of WT protein. ... indeed has an affinity for copper(I) (...) higher than that of the P174L-HSco1 mutant but lower than that...
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pubNational Academy of Sciences
urlhttp://search.proquest.com/docview/201320543/
doi10.1073/pnas.0606189103
date2007-01-02