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

Proton-coupled electron transfer at the Q(o) site: what type of mechanism can account for the high activation barrier?

Biochimica et biophysica acta - 15 Aug 2000

Crofts A R, Guergova-Kuras M, Kuras R, Ugulava N, Li J, Hong S

Abstract excerpt

In Rhodobacter sphaeroides, transfer of the first electron in quinol oxidation by the bc(1) complex shows kinetic features (a slow rate (approx. 1.5 x 10(3)/s), high activation energy (approx. 65 kJ/mol) and reorganization energy, lambda (2.5 V)) that are unexpected from Marcus theory and the distances shown by the structures. Reduction of the oxidized iron-sulfur protein occurs after formation of the...

Read the complete abstract on PubMed

Topics

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

Share to Electron Spin Resonance Spectroscopy
Share to Electron Transport

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Electron Transport Complex III

Share to Iron-Sulfur Proteins

Share to Models, Chemical

Share to Protons

Share to Rhodobacter sphaeroides

Share to Thiazoles

Source

Identifiers

PMID: 11004463
DOI: 10.1016/s0005-2728(00)00184-5

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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

Proton-coupled electron transfer at the Q(o) site: what type of mechanism can account for the high activation barrier?PMID 11004463Read ↗

Proton-coupled electron transfer at the Qo-site of the bc1 complex controls the rate of ubihydroquinone oxidation.Semantic proximity Read ↗

The mechanism of ubihydroquinone oxidation at the Qo-site of the cytochrome bc1 complex.Semantic proximity Read ↗

Protonated rhodosemiquinone at the Q(B) binding site of the M265IT mutant reaction center of photosynthetic bacterium Rhodobacter sphaeroides.Semantic proximity Read ↗

Proton and electron transfer in bacterial reaction centers.Semantic proximity Read ↗

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

Reduction and protonation of the secondary quinone acceptor of Rhodobacter sphaeroides photosynthetic reaction center: kinetic model based on a comparison of wild-type chromatophores with mutants carrying Arg-->Ile substitution at sites 207 and 217 in the L-subunit.Semantic proximity Read ↗

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

Role of protein dynamics in guiding electron-transfer pathways in reaction centers from Rhodobacter sphaeroides.Semantic proximity Read ↗

Identification of the proton pathway in bacterial reaction centers: replacement of Asp-M17 and Asp-L210 with asn reduces the proton transfer rate in the presence of Cd2+.Semantic proximity Read ↗

Photoinduced electron transfer between the Rieske iron-sulfur protein and cytochrome c(1) in the Rhodobacter sphaeroides cytochrome bc(1) complex. Effects of pH, temperature, and driving force.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 ↗

Proton transfer in uncoupled variants of cytochrome c oxidase.Semantic proximity Read ↗

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