A tyrosine residue deprotonates during oxygen reduction by the caa3 reductase from Rhodothermus marinus

Manuela M. Pereira, Filipa L. Sousa, Miguel Teixeira, Rebecca M. Nyquist, Joachim Heberle

Research output: Contribution to journalArticle

21 Citations (Scopus)

Abstract

Heme-copper oxygen reductases catalyze proton translocation across the cellular membrane; this takes place during the reaction of oxygen to water. We demonstrate with attenuated total reflection-Fourier transform infrared (ATR-FTIR) difference spectroscopy that a tyrosine residue of the oxygen reductase from the thermohalophilic Rhodothermus marinus becomes deprotonated in the transition from the oxidized state to the catalytic intermediate ferryl state PM. This tyrosine residue is most probably Y256, the helix VI tyrosine residue proposed to substitute for the D-channel glutamic acid that is absent in this enzyme. Comparison with the mitochondrial like oxygen reductase from Rhodobacter sphaeroides suggests that proton transfer from a strategically situated donor to the active site is a crucial step in the reaction mechanism of oxygen reductases.

Original languageEnglish
Pages (from-to)1350-1354
Number of pages5
JournalFEBS Letters
Volume580
Issue number5
DOIs
Publication statusPublished - 20 Feb 2006

Keywords

  • Bacteriorhodopsin
  • Cytochrome c oxidase
  • Electron transfer
  • FTIR
  • Glutamic acid
  • Membrane
  • Proton translocation
  • Respiration
  • Tyrosine
  • Vibrational spectroscopy

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