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

Surface proton donors for the D-pathway of cytochrome c oxidase in the absence of subunit III.

Biochemistry - 11 Jul 2006

Adelroth Pia, Hosler Jonathan

Abstract excerpt

The major proton-transfer pathway into the buried active site of cytochrome c oxidase (CcO) is the D-pathway that begins with the subunit I residue Asp-132 on the inner protein surface (the cytoplasmic surface of the aa3-type CcO of Rhodobacter sphaeroides). Asp-132 is surrounded by residues from both subunits I and III. In the absence of subunit III, CcO retains activity, but the functional characteristics of...

Read the complete abstract on PubMed

Topics

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

Share to Arachidonic Acid
Share to Asparagine
Share to Catalysis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Electron Transport Complex IV

Share to Oxygen

Share to Protein Subunits

Share to Protons

Share to Rhodobacter sphaeroides

Source

Identifiers

PMID: 16819830
DOI: 10.1021/bi0605843

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Surface proton donors for the D-pathway of cytochrome c oxidase in the absence of subunit III.PMID 16819830Read ↗

Alternative initial proton acceptors for the D pathway of Rhodobacter sphaeroides 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 ↗

Replacing Asn207 by aspartate at the neck of the D channel in the aa3-type cytochrome c oxidase from Rhodobacter sphaeroides results in decoupling the proton pump.Semantic proximity Read ↗

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

On the role of the K-proton transfer pathway in cytochrome c oxidase.Semantic proximity Read ↗

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

Where is 'outside' in cytochrome c oxidase and how and when do protons get there?Semantic proximity Read ↗

Relocation of an internal proton donor in cytochrome c oxidase results in an altered pK(a) and a non-integer pumping stoichiometry.Semantic proximity Read ↗

Crystallographic location and mutational analysis of Zn and Cd inhibitory sites and role of lipidic carboxylates in rescuing proton path mutants in cytochrome c oxidase.Semantic proximity Read ↗

Energetics of proton transfer pathways in reaction centers from Rhodobacter sphaeroides. The Glu-H173 activated mutants.Semantic proximity Read ↗

Proton transfer from glutamate 286 determines the transition rates between oxygen intermediates in cytochrome c oxidase.Semantic proximity Read ↗

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