ArticleProceedings of the National Academy of Sciences of the United States of America2009
The cytochrome ba3 oxygen reductase from Thermus thermophilus uses a single input channel for proton delivery to the active site and for proton pumping.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed, 110 citations in OpenAlex.
- The three-dimensional structure of a proton-pumping pathway, the H-pathway, is evolutionarily conserved in all three families of cytochromeFrontiers in chemistry · 2025Article
- Diversity and evolution of nitric oxide reduction in bacteria and archaea.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Time-resolved serial crystallography to track the dynamics of carbon monoxide in the active site of cytochromeScience advances · 2023Article
- A simple goniometer-compatible flow cell for serial synchrotron X-ray crystallography.Journal of applied crystallography · 2023Article
- Reaction pathways, proton transfer, and proton pumping in ba3 class cytochrome c oxidase: perspectives from DFT quantum chemistry and molecular dynamics.Frontiers in chemistry · 2023Article
- The Unusual Homodimer of a Heme-Copper Terminal Oxidase Allows Itself to Utilize Two Electron Donors.Angewandte Chemie (International ed. in English) · 2021Article
- Architecture of bacterial respiratory chains.Nature reviews. Microbiology · 2021Review
- Molecular understanding of heteronuclear active sites in heme-copper oxidases, nitric oxide reductases, and sulfite reductases through biomimetic modelling.Chemical Society reviews · 2021Review
- Coupled transport of electrons and protons in a bacterial cytochromePhysical chemistry chemical physics : PCCP · 2020Article
- Proton-transfer pathways in the mitochondrial S. cerevisiae cytochrome c oxidase.Scientific reports · 2019Article
- Mechanism of proton transfer through the KBiochimica et biophysica acta. Bioenergetics · 2018Article
- Bacterial denitrifying nitric oxide reductases and aerobic respiratory terminal oxidases use similar delivery pathways for their molecular substrates.Biochimica et biophysica acta. Bioenergetics · 2018Article
- Dewetting transitions coupled to K-channel activation in cytochromeChemical science · 2018Article
- Cytochrome aaBiochemistry · 2018Article
- Oxygen Activation and Energy Conservation by Cytochrome c Oxidase.Chemical reviews · 2018Review
- Characterization of the quinol-dependent nitric oxide reductase from the pathogen Neisseria meningitidis, an electrogenic enzyme.Scientific reports · 2018Article
- Serial femtosecond crystallography structure of cytochrome c oxidase at room temperature.Scientific reports · 2017Article
- Splitting of the O-O bond at the heme-copper catalytic site of respiratory oxidases.Science advances · 2017Article
- The cellular membrane as a mediator for small molecule interaction with membrane proteins.Biochimica et biophysica acta · 2016Article
- Water exit pathways and proton pumping mechanism in B-type cytochrome c oxidase from molecular dynamics simulations.Biochimica et biophysica acta · 2016Article
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
The heme-copper oxygen reductases are redox-driven proton pumps that generate a proton motive force in both prokaryotes and mitochondria. These enzymes have been divided into 3 evolutionarily related groups: the A-, B- and C-families. Most experimental work on proton-pumping mechanisms has been performed with members of the A-family. These enzymes require 2 proton input pathways (D- and K-channels) to transfer protons used for oxygen reduction chemistry and for proton pumping, with the D-channel transporting all pumped protons. In this work we use site-directed mutagenesis to demonstrate that the ba(3) oxygen reductase from Thermus thermophilus, a representative of the B-family, does not contain a D-channel. Rather, it utilizes only 1 proton input channel, analogous to that of the A-family K-channel, and it delivers protons to the active site for both O2 chemistry and proton pumping. Comparison of available subunit I sequences reveals that the only structural elements conserved within the oxygen reductase families that could perform these functions are active-site components, namely the covalently linked histidine-tyrosine, the Cu(B) and its ligands, and the active-site heme and its ligands. Therefore, our data suggest that all oxygen reductases perform the same chemical reactions for oxygen reduction and comprise the essential elements of the proton-pumping mechanism (e.g., the proton-loading and kinetic-gating sites). These sites, however, cannot be located within the D-channel. These results along with structural considerations point to the A-propionate region of the active-site heme and surrounding water molecules as the proton-loading site.
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