umu.sePublications
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Role of metal in folding and stability of copper proteins in vitro
Umeå University, Faculty of Science and Technology, Department of Chemistry. (Chemical Biological Center)
Umeå University, Faculty of Science and Technology, Department of Chemistry. (Chemical Biological Center)
Umeå University, Faculty of Science and Technology, Department of Chemistry.
2012 (English)In: Biochimica et Biophysica Acta. Molecular Cell Research, ISSN 0167-4889, E-ISSN 1879-2596, Vol. 1823, no 9, 1594-1603 p.Article, review/survey (Refereed) Published
Abstract [en]

Metal coordination is required for function of many proteins. For biosynthesis of proteins coordinating a metal, the question arises if the metal binds before, during or after folding of the polypeptide. Moreover, when the metal is bound to the protein, how does its coordination affect biophysical properties such as stability and dynamics? Understanding how metals are utilized by proteins in cells on a molecular level requires accurate descriptions of the thermodynamic and kinetic parameters involved in protein-metal complexes. Copper is one of the essential transition metals found in the active sites of many key proteins. To avoid toxicity of free copper ions, living systems have developed elaborate copper-transport systems that involve dedicated proteins that facilitate efficient and specific delivery of copper to target proteins. This review describes in vitro and in silico biophysical work assessing the role of copper in folding and stability of copper-binding proteins. Examples of proteins discussed are: a blue-copper protein (Pseudomonas aeruginosa azurin), members of copper-transport systems (bacterial CopZ, human Atox1 and ATP7B domains) and multi-copper ferroxidases (yeast Fet3p and human ceruloplasmin). The consequences of interactions between copper proteins and platinum-complexes are also discussed. 

Place, publisher, year, edition, pages
Amsterdam: Elsevier, 2012. Vol. 1823, no 9, 1594-1603 p.
Keyword [en]
Protein folding, Azurin, Atox1, Ceruloplasmin, Wilson disease protein, Cisplatin
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:umu:diva-54418DOI: 10.1016/j.bbamcr.2012.01.013ISI: 000307918100018PubMedID: 22306006OAI: oai:DiVA.org:umu-54418DiVA: diva2:523740
Note

Special issue: Cell Biology of Metals

Available from: 2012-04-26 Created: 2012-04-26 Last updated: 2017-12-07Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full textPubMed

Search in DiVA

By author/editor
Palm-Espling, Maria ENiemiec, Moritz SWittung-Stafshede, Pernilla
By organisation
Department of Chemistry
In the same journal
Biochimica et Biophysica Acta. Molecular Cell Research
Biochemistry and Molecular Biology

Search outside of DiVA

GoogleGoogle Scholar

doi
pubmed
urn-nbn

Altmetric score

doi
pubmed
urn-nbn
Total: 135 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf