Structural insights into functional properties of the oxidized form of cytochrome c oxidase

Izumi Ishigami, Raymond G. Sierra, Zhen Su, Ariana Peck, Cong Wang, Frederic Poitevin, Stella Lisova, Brandon Hayes, Frank R. Moss, Sébastien Boutet, Robert E. Sublett, Chun Hong Yoon, Syun-Ru Yeh () and Denis L. Rousseau ()
Additional contact information
Izumi Ishigami: Albert Einstein College of Medicine
Raymond G. Sierra: SLAC National Accelerator Laboratory
Zhen Su: SLAC National Accelerator Laboratory
Ariana Peck: SLAC National Accelerator Laboratory
Cong Wang: SLAC National Accelerator Laboratory
Frederic Poitevin: SLAC National Accelerator Laboratory
Stella Lisova: SLAC National Accelerator Laboratory
Brandon Hayes: SLAC National Accelerator Laboratory
Frank R. Moss: SLAC National Accelerator Laboratory
Sébastien Boutet: SLAC National Accelerator Laboratory
Robert E. Sublett: SLAC National Accelerator Laboratory
Chun Hong Yoon: SLAC National Accelerator Laboratory
Syun-Ru Yeh: Albert Einstein College of Medicine
Denis L. Rousseau: Albert Einstein College of Medicine

Nature Communications, 2023, vol. 14, issue 1, 1-10

Abstract: Abstract Cytochrome c oxidase (CcO) is an essential enzyme in mitochondrial and bacterial respiration. It catalyzes the four-electron reduction of molecular oxygen to water and harnesses the chemical energy to translocate four protons across biological membranes. The turnover of the CcO reaction involves an oxidative phase, in which the reduced enzyme (R) is oxidized to the metastable OH state, and a reductive phase, in which OH is reduced back to the R state. During each phase, two protons are translocated across the membrane. However, if OH is allowed to relax to the resting oxidized state (O), a redox equivalent to OH, its subsequent reduction to R is incapable of driving proton translocation. Here, with resonance Raman spectroscopy and serial femtosecond X-ray crystallography (SFX), we show that the heme a3 iron and CuB in the active site of the O state, like those in the OH state, are coordinated by a hydroxide ion and a water molecule, respectively. However, Y244, critical for the oxygen reduction chemistry, is in the neutral protonated form, which distinguishes O from OH, where Y244 is in the deprotonated tyrosinate form. These structural characteristics of O provide insights into the proton translocation mechanism of CcO.

Date: 2023
References: View references in EconPapers View complete reference list from CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-023-41533-x Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-41533-x

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-023-41533-x

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().