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

Effects of site-directed mutagenesis of protolytic residues in subunit I of Bacillus subtilis aa3-600 quinol oxidase. Role of lysine 304 in proton translocation.

Biochemistry - 23 Feb 1999

Villani G, Capitanio N, Bizzoca A, Palese L L, Carlino V, Tattoli M, Glaser P, Danchin A, Papa S

Abstract excerpt

Various protolytic residues in subunit I of aa3-600 quinol oxidase of the aerobic Gram-positive Bacillus subtilis were mutagenized to nonpolar residues. Two of the mutations, Y284F and K304L, impaired the bioenergetic function of the microorganism. The Y284F mutation suppressed the electron-transfer activity of quinol oxidase and altered its interaction with CO and H2O2, thus showing destruction of the binuclear...

Read the complete abstract on PubMed

Topics

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

Share to Bacillus subtilis
Share to Biological Transport

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Catalysis

Share to Electron Transport Complex IV

Share to Lysine

Share to Oxidoreductases

Share to Proton-Motive Force

Share to Protons

Source

Identifiers

PMID: 10029521
DOI: 10.1021/bi980774g

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

Effects of site-directed mutagenesis of protolytic residues in subunit I of Bacillus subtilis aa3-600 quinol oxidase. Role of lysine 304 in proton translocation.PMID 10029521Read ↗

Cytochrome c oxidase (heme aa3) from Paracoccus denitrificans: analysis of mutations in putative proton channels of subunit I.Semantic proximity Read ↗

Electron transfer processes in subunit I mutants of cytochrome bo quinol oxidase in Escherichia coli.Semantic proximity Read ↗

Effects of subunit I mutations on redox-linked conformational changes of the Escherichia coli bo-type ubiquinol oxidase revealed by Fourier-transform infrared spectroscopy.Semantic proximity Read ↗

Differential effects of glutamate-286 mutations in the aa(3)-type cytochrome c oxidase from Rhodobacter sphaeroides and the cytochrome bo(3) ubiquinol oxidase from Escherichia coli.Semantic proximity Read ↗

Mutation analysis of the interaction of B-type cytochrome c oxidase with its natural substrate cytochrome c-551.Semantic proximity Read ↗

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

Allosteric interactions and proton conducting pathways in proton pumping aa(3) oxidases: heme a as a key coupling element.Semantic proximity Read ↗

Effect of mutations of five conserved histidine residues in the catalytic subunit of the cbb3 cytochrome c oxidase on its function.Semantic proximity Read ↗

Functional effects of mutations in cytochrome c oxidase related to prostate cancer.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 ↗

The causes of reduced proton-pumping efficiency in type B and C respiratory heme-copper oxidases, and in some mutated variants of type A.Semantic proximity Read ↗

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

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