A heme-based redox sensor in the methanogenic archaeon methanosarcina acetivorans

Research output: Contribution to journalResearch articleContributedpeer-review

Contributors

  • Bastian Molitor - , Ruhr University Bochum (Author)
  • Marc Stassen - , Ruhr University Bochum (Author)
  • Anuja Modi - , University Hospital Frankfurt (Author)
  • Samir F. El-Mashtoly - , University of South Carolina (Author)
  • Christoph Laurich - , Max Planck Institute for Chemical Energy Conversion (Author)
  • Wolfgang Lubitz - , Max Planck Institute for Chemical Energy Conversion (Author)
  • John H. Dawson - , University Hospital Frankfurt (Author)
  • Michael Rother - , Ruhr University Bochum, TUD Dresden University of Technology (Author)
  • Nicole Frankenberg-Dinkel - , Ruhr University Bochum (Author)

Abstract

Background: Multidomain sensory kinases are involved in numerous receptive processes in all kingdoms of life. Results: The multidomain sensory kinase MA4561 covalently binds a redox-active heme cofactor, which triggers kinase activity. Conclusion: Covalently bound heme is utilized to detect redox changes. Significance: Learning how Archaea perceive environmental stimuli will enhance our understanding of the evolution of prokaryotic signal transduction.

Details

Original languageEnglish
Pages (from-to)18458-18472
Number of pages15
JournalJournal of Biological Chemistry
Volume288
Issue number25
Publication statusPublished - 21 Jun 2013
Peer-reviewedYes
Externally publishedYes

External IDs

PubMed 23661702

Keywords