Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Insights into proton translocation in cbb3 oxidase from MD simulations.

Biochimica et biophysica acta. Bioenergetics - 1 May 2017

Carvalheda Catarina A, Pisliakov Andrei V

Abstract excerpt

Heme-copper oxidases are membrane protein complexes that catalyse the final step of the aerobic respiration, namely the reduction of oxygen to water. The energy released during catalysis is coupled to the active translocation of protons across the membrane, which contributes to the establishment of an electrochemical gradient that is used for ATP synthesis. The distinctive C-type (or cbb3) cytochrome c oxidases,...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Electron Transport Complex IV
Share to Energy Metabolism
Share to Lipid Bilayers

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Oxygen

Share to Proton Pumps

Share to Protons

Share to Solvents

Source

Identifiers

PMID: 28259641
DOI: 10.1016/j.bbabio.2017.02.013

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Insights into proton translocation in cbb3 oxidase from MD simulations.PMID 28259641Read ↗

Intricate role of water in proton transport through cytochrome c oxidase.Semantic proximity Read ↗

Conformational coupling between the active site and residues within the K(C)-channel of the Vibrio cholerae cbb3-type (C-family) oxygen reductase.Semantic proximity Read ↗

Understanding the essential proton-pumping kinetic gates and decoupling mutations in cytochrome c oxidase.Semantic proximity Read ↗

Decoupling mutations in the D-channel of the aa(3)-type cytochrome c oxidase from Rhodobacter sphaeroides suggest that a continuous hydrogen-bonded chain of waters is essential for proton pumping.Semantic proximity Read ↗

Kinetic gating of the proton pump in cytochrome c oxidase.Semantic proximity Read ↗

Subunit III-depleted cytochrome c oxidase provides insight into the process of proton uptake by proteins.Semantic proximity Read ↗

Structural elements involved in proton translocation by cytochrome c oxidase as revealed by backbone amide hydrogen-deuterium exchange of the E286H mutant.Semantic proximity Read ↗

Electrostatic control of proton pumping in cytochrome c oxidase.Semantic proximity Read ↗

"Proton holes" in long-range proton transfer reactions in solution and enzymes: A theoretical analysis.Semantic proximity Read ↗

Single-Amino Acid Modifications Reveal Additional Controls on the Proton Pathway of [FeFe]-Hydrogenase.Semantic proximity Read ↗

Mutation of a single residue in the ba3 oxidase specifically impairs protonation of the pump site.Semantic proximity Read ↗

Proton-assisted two-electron transfer in natural variants of tetraheme cytochromes from Desulfomicrobium Sp.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.