Biophysical characterization of iron-sulfur proteins

Bhanu P. Jagilinki, Irina Paluy, Alexei M. Tyryshkin, Vikas Nanda, Dror Noy

Research output: Contribution to journalArticlepeer-review

Abstract

Iron-sulfur proteins are primordial catalysts and biological electron carriers that today drive major metabolic pathways across all forms of life. They can access a diversity of oxidation states and can mediate electron transfer over an extended range of reduction potentials spanning more than 1 V. Depending on the protein micro-environment and geometry of ligand, co-ordination the iron-sulfur clusters can occur in different forms [2Fe-2S], [3Fe-4S], HiPIP [4Fe-4S], and [4Fe-4S]. There are several spectroscopic methods available to characterize the composition and electronic configuration of the iron-sulfur clusters, such as optical methods and electron paramagnetic resonance. This paper presents the protocols used to characterize the metal center of Coiled-Coil Iron-Sulfur (CCIS), an artificial metalloprotein containing one [4Fe-4S] cluster. It is expected that these protocols will be of general utility for other iron-sulfur proteins.

Original languageEnglish (US)
Article numbere4202
JournalBio-protocol
Volume11
Issue number20
DOIs
StatePublished - Oct 20 2021
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)
  • Neuroscience(all)
  • Plant Science

Keywords

  • Electron paramagnetic resonance
  • ICP-AES
  • Iron-sulfur proteins
  • UV-visible spectroscopy
  • [4Fe-4S] clusters

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