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

On the rate of proton exchange with solvent of the catalytic histidine in flavocytochrome b2 (yeast L-lactate dehydrogenase).

Protein science : a publication of the Protein Society - 1 Jan 1994

Balme A, Lederer F

Abstract excerpt

The family of FMN-dependent, alpha-hydroxy acid-oxidizing enzymes catalyzes substrate dehydrogenation by a mechanism the first step of which is abstraction of the substrate alpha-proton (so-called carbanion mechanism). For flavocytochrome b2 and lactate oxidase, it was shown that once on the enzyme this proton is lost only slowly to the solvent (Lederer F, 1984, In: Bray RC, Engel PC, Mayhew SG, eds, Flavins &...

Read the complete abstract on PubMed

Topics

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

Share to Escherichia coli
Share to Histidine
Share to Hydrogen Bonding

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

Share to Kinetics

Share to Molecular Structure

Share to Mutation

Share to Recombinant Proteins

Share to Saccharomyces cerevisiae

Source

Open in PubMed Open full text

Identifiers

PMID: 8142887
DOI: 10.1002/pro.5560030114
PMCID: PMC2142476

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

On the rate of proton exchange with solvent of the catalytic histidine in flavocytochrome b2 (yeast L-lactate dehydrogenase).PMID 8142887Read ↗

The catalytic role of tyrosine 254 in flavocytochrome b2 (L-lactate dehydrogenase from baker's yeast). Comparison between the Y254F and Y254L mutant proteins.Semantic proximity Read ↗

Role of active site residues and solvent in proton transfer and the modulation of flavin reduction potential in bacterial morphinone reductase.Semantic proximity Read ↗

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

Environmental Contributions to Proton Sharing in Protein Low-Barrier Hydrogen BondsSemantic proximity Read ↗

Deletions in the interdomain hinge region of flavocytochrome b2: effects on intraprotein electron transfer.Semantic proximity Read ↗

On the role of Brønsted catalysis in Pseudomonas fluorescens mannitol 2-dehydrogenase.Semantic proximity Read ↗

The Redox-Bohr group associated with iron-sulfur cluster N2 of complex I.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 ↗

Single-Amino Acid Modifications Reveal Additional Controls on the Proton Pathway of [FeFe]-Hydrogenase.Semantic proximity Read ↗

In Rhodobacter sphaeroides reaction centers, mutation of proline L209 to aromatic residues in the vicinity of a water channel alters the dynamic coupling between electron and proton transfer processes.Semantic proximity Read ↗

Proton transfer pathways in the mutant His-64-Ala of human carbonic anhydrase II.Semantic proximity Read ↗

X-ray structures of Aerococcus viridans lactate oxidase and its complex with D-lactate at pH 4.5 show an alpha-hydroxyacid oxidation mechanism.Semantic proximity Read ↗

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