Good and bad of Cu/Zn-superoxide dismutase controlled by metal ions and disulfide bonds

Research output: Contribution to journalReview articlepeer-review

9 Citations (Scopus)

Abstract

Cu/Zn-superoxide dismutase (SOD1) is a metalloenzyme that catalyzes the disproportionation of superoxide. This review summarizes intracellular processes for metal binding and disulfide formation in SOD1, both of which are essential to stabilization of the protein structure as well as its enzymatic function. Also, failure of those processes as a possible cause of a neurodegenerative disease through protein misfolding will be described.

Original languageEnglish
Pages (from-to)331-341
Number of pages11
JournalChemistry Letters
Volume50
Issue number2
DOIs
Publication statusPublished - 2021

Keywords

  • Metalloprotein
  • Neurodegenerative disease
  • Protein folding

ASJC Scopus subject areas

  • General Chemistry

Fingerprint

Dive into the research topics of 'Good and bad of Cu/Zn-superoxide dismutase controlled by metal ions and disulfide bonds'. Together they form a unique fingerprint.

Cite this