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

F1-ATPase with cysteine instead of serine at residue 373 of the alpha subunit.

Archives of biochemistry and biophysics - 1 Sept 1992

Lee R S, Wilke-Mounts S, Senior A E

Abstract excerpt

Escherichia coli strain AN718 contains the alpha S373F mutation in F1F0-ATP synthase which blocks ATP synthesis (oxidative phosphorylation) and steady-state F1-ATPase activity. The revertant strain AN718SS2 containing the mutation alpha C373 was isolated and shown to confer a phenotype of higher growth yield than that of the wild type in liquid medium containing limiting glucose, succinate, or LB. Purified F1...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Cell Membrane
Share to Cysteine

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Escherichia coli

Share to Genotype

Share to Kinetics

Share to Macromolecular Substances

Share to Species Specificity

Source

Identifiers

PMID: 1386722
DOI: 10.1016/0003-9861(92)90681-l

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. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

F1-ATPase with cysteine instead of serine at residue 373 of the alpha subunit.PMID 1386722Read ↗

Conformational changes in the Escherichia coli ATP synthase (ECF1F0) monitored by nucleotide-dependent differences in the reactivity of Cys-87 of the gamma subunit in the mutant betaGlu-381 --> Ala.Semantic proximity Read ↗

Tryptophan-free Escherichia coli F1-ATPase.Semantic proximity Read ↗

Role of {alpha}-subunit VISIT-DG sequence residues Ser-347 and Gly-351 in the catalytic sites of Escherichia coli ATP synthase.Semantic proximity Read ↗

The Escherichia coli F1-ATPase mutant beta Tyr-297-->Cys: functional studies and asymmetry of the enzyme under various nucleotide conditions based on reaction of the introduced Cys with N-ethylmaleimide and 7-chloro-4-nitrobenzofurazan.Semantic proximity Read ↗

Further examination of seventeen mutations in Escherichia coli F1-ATPase beta-subunit.Semantic proximity Read ↗

Role of alphaPhe-291 residue in the phosphate-binding subdomain of catalytic sites of Escherichia coli ATP synthase.Semantic proximity Read ↗

Catalytic site of F1-ATPase of Escherichia coli. Lys-155 and Lys-201 of the beta subunit are located near the gamma-phosphate group of ATP in the presence of Mg2+.Semantic proximity Read ↗

Significance of αThr-349 in the catalytic sites of Escherichia coli ATP synthase.Semantic proximity Read ↗

ATP hydrolysis-driven structural changes in the gamma-subunit of Escherichia coli ATPase monitored by fluorescence from probes bound at introduced cysteine residues.Semantic proximity Read ↗

alpha-Aspartate 261 is a key residue in noncatalytic sites of Escherichia coli F1-ATPase.Semantic proximity Read ↗

N-ethylmaleimide-sensitive mutant (beta Val-153-->Cys) Escherichia coli F1-ATPase: cross-linking of the mutant beta subunit with the alpha subunit.Semantic proximity Read ↗

On the role of Arg-210 and Glu-219 of subunit a in proton translocation by the Escherichia coli F0F1-ATP synthase.Semantic proximity Read ↗

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