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

Aqueous access pathways in ATP synthase subunit a. Reactivity of cysteine substituted into transmembrane helices 1, 3, and 5.

The Journal of biological chemistry - 23 Mar 2007

Angevine Christine M, Herold Kelly A G, Vincent Owen D, Fillingame Robert H

Abstract excerpt

Subunit a is thought to play a key role in H+ transport-driven rotation of the subunit c ring in Escherichia coli F1F0 ATP synthase. In the membrane-traversing F0 sector of the enzyme, H+ binding and release occurs at Asp-61 in the middle of the second transmembrane helix (TMH) of subunit c. Protons are thought to reach Asp-61 via aqueous channels formed at least in part by one or more of the five TMHs of subunit...

Read the complete abstract on PubMed

Topics

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

Share to Aspartic Acid
Share to Cysteine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cytoplasm

Share to Ethylmaleimide

Share to Proton-Translocating ATPases

Share to Protons

Share to Silver

Source

Identifiers

PMID: 17234633
DOI: 10.1074/jbc.M610848200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Aqueous access pathways in ATP synthase subunit a. Reactivity of cysteine substituted into transmembrane helices 1, 3, and 5.PMID 17234633Read ↗

Aqueous access pathways in subunit a of rotary ATP synthase extend to both sides of the membrane.Semantic proximity Read ↗

Structural interactions between transmembrane helices 4 and 5 of subunit a and the subunit c ring of Escherichia coli ATP synthase.Semantic proximity Read ↗

Conserved Asp684 in transmembrane segment M6 of the plant plasma membrane P-type proton pump AHA2 is a molecular determinant of proton translocation.Semantic proximity Read ↗

Structural model of the transmembrane Fo rotary sector of H+-transporting ATP synthase derived by solution NMR and intersubunit cross-linking in situ.Semantic proximity Read ↗

Transmembrane helix-helix interactions in F0 suggested by suppressor mutations to Ala24-->Asp/Asp61-->Gly mutant of ATP synthase subunit.Semantic proximity Read ↗

A model for the structure of subunit a of the Escherichia coli ATP synthase and its role in proton translocation.Semantic proximity Read ↗

The Xenobiotic Extrusion Mechanism of the MATE Transporter NorM_PS from Pseudomonas stutzeri.Semantic proximity Read ↗

Cysteine-scanning mutagenesis and thiol modification of the Rickettsia prowazekii ATP/ADP translocase: evidence that transmembrane regions I and II, but not III, are structural components of the aqueous translocation channel.Semantic proximity Read ↗

Disulfide linkage in the coiled-coil domain of subunit H of A1AO ATP synthase from Methanocaldococcus jannaschii and the NMR structure of the C-terminal segment H(85-104).Semantic proximity Read ↗

Modulation of charge in the phosphate binding site of Escherichia coli ATP synthase.Semantic proximity Read ↗

Identification of a region involved in the communication between the NADP(H) binding domain and the membrane domain in proton pumping E. coli transhydrogenase.Semantic proximity Read ↗

Substrate binding, deprotonation, and selectivity at the periplasmic entrance of the Escherichia coli ammonia channel AmtB.Semantic proximity Read ↗

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