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

Peroxynitrite isomerization catalyzed by his64 myoglobin mutants.

Journal of the American Chemical Society - 2 May 2001

Herold S, Matsui T, Watanabe Y

Abstract excerpt

No abstract is available from the source.

Read the complete abstract on PubMed

Topics

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

Share to Isomerism
Share to Mutation
Share to Myoglobin
Share to Nitrates

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Spectrophotometry, Ultraviolet

Share to Whales

Source

Identifiers

PMID: 11457162
DOI: 10.1021/ja010111d

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

Peroxynitrite isomerization catalyzed by his64 myoglobin mutants.PMID 11457162Read ↗

Mechanistic studies of the isomerization of peroxynitrite to nitrate catalyzed by distal histidine metmyoglobin mutants.Semantic proximity Read ↗

Pseudoperoxidase activity, conformational stability, and aggregation propensity of the His98Tyr myoglobin variant: implications for the onset of myoglobinopathy.Semantic proximity Read ↗

Effect of distal histidines on hydrogen peroxide activation by manganese reconstituted myoglobin.Semantic proximity Read ↗

Molecular basis for the resistance of human mitochondrial 2-Cys peroxiredoxin 3 to hyperoxidation.Semantic proximity Read ↗

Peroxynitrite-mediated oxidation of the C85S/C152E mutant of dihydrofolate reductase from Escherichia coli: functional and structural effects.Semantic proximity Read ↗

Catalase reaction by myoglobin mutants and native catalase: mechanistic investigation by kinetic isotope effect.Semantic proximity Read ↗

Monooxygenation of an aromatic ring by F43W/H64D/V68I myoglobin mutant and hydrogen peroxide. Myoglobin mutants as a model for P450 hydroxylation chemistry.Semantic proximity Read ↗

Investigations of the roles of the distal heme environment and the proximal heme iron ligand in peroxide activation by heme enzymes via molecular engineering of myoglobin.Semantic proximity Read ↗

Quaternary structure influences the peroxidase activity of peroxiredoxin 3.Semantic proximity Read ↗

Structural insights into the peroxidase activity and inactivation of human peroxiredoxin 4.Semantic proximity Read ↗

Role of tyrosine-103 in myoglobin peroxidase activity: kinetic and steady-state studies on the reaction of wild-type and variant recombinant human myoglobins with H(2)O(2).Semantic proximity Read ↗

Real-time monitoring of peroxiredoxin oligomerization dynamics in living cells.Semantic proximity Read ↗

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