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

1H NMR studies on the CuA center of nitrous oxide reductase from Pseudomonas stutzeri.

Biochemistry - 24 Aug 1999

Holz R C, Alvarez M L, Zumft W G, Dooley D M

Abstract excerpt

1H NMR spectra of the CuA center of N2OR from Pseudomonas stutzeri, and a mutant enzyme that contains only CuA, were recorded in both H2O- and D2O-buffered solution at pH 7.5. Several sharp, well-resolved hyperfine-shifted 1H NMR signals were observed in the 60 to -10 ppm chemical shift range. Comparison of the native and mutant N2OR spectra recorded in H2O-buffered solutions indicated that several additional...

Read the complete abstract on PubMed

Topics

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

Share to Copper
Share to Electron Transport
Share to Hydrogen-Ion Concentration

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

Share to Nuclear Magnetic Resonance, Biomolecular

Share to Oxidoreductases

Share to Peptide Fragments

Share to Protons

Share to Pseudomonas

Source

Identifiers

PMID: 10460173
DOI: 10.1021/bi990595e

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

1H NMR studies on the CuA center of nitrous oxide reductase from Pseudomonas stutzeri.PMID 10460173Read ↗

CuA and CuZ are variants of the electron transfer center in nitrous oxide reductase.Semantic proximity Read ↗

Electron spin-lattice relaxation of the [Cu(1.5) ... Cu(1.5)] dinuclear copper center in nitrous oxide reductase.Semantic proximity Read ↗

Two cysteines, two histidines, and one methionine are ligands of a binuclear purple copper center.Semantic proximity Read ↗

Femtosecond serial crystallography of two classes of copper nitrite reductaseSemantic proximity Read ↗

Molecular characterization of nosA, a Pseudomonas stutzeri gene encoding an outer membrane protein required to make copper-containing N2O reductase.Semantic proximity Read ↗

Crystallization and preliminary X-ray crystallographic studies of dissimilatory nitrite reductase isolated from Hyphomicrobium denitrificans A3151.Semantic proximity Read ↗

1H NMR studies of the paramagnetic CuA center of cytochrome oxidase.Semantic proximity Read ↗

Role of the Tat ransport system in nitrous oxide reductase translocation and cytochrome cd1 biosynthesis in Pseudomonas stutzeri.Semantic proximity Read ↗

Conformation of pseudoazurin in the 152 kDa electron transfer complex with nitrite reductase determined by paramagnetic NMR.Semantic proximity Read ↗

Site-directed mutagenesis reveals a conservation of the copper-binding site and the crucial role of His24 in CopH from Cupriavidus metallidurans CH34.Semantic proximity Read ↗

NMR studies of recombinant Coprinus peroxidase and three site-directed mutants. Implications for peroxidase substrate binding.Semantic proximity Read ↗

Effects of substrates (methyl isocyanide, C2H2) and inhibitor (CO) on resting-state wild-type and NifV(-)Klebsiella pneumoniae MoFe proteins.Semantic proximity Read ↗

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