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

Dependence of catalytic activity on driving force in solution assays and protein film voltammetry: insights from the comparison of nitrate reductase mutants.

Biochemistry - 23 Mar 2010

Fourmond Vincent, Burlat Bénédicte, Dementin Sébastien, Sabaty Monique, Arnoux Pascal, Etienne Emilien, Guigliarelli Bruno, Bertrand Patrick, Pignol David, Léger Christophe

Abstract excerpt

Rhodobacter sphaeroides periplasmic nitrate reductase (Rs NapAB) is one of the enzymes whose assays give odd results: in spectrophotometric assays with methyl viologen as the electron donor, the activity increases as the reaction progresses, whereas the driving force provided by the soluble redox...

Read the complete abstract on PubMed

Topics

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

Share to Biocatalysis
Share to Electrochemistry

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutant Proteins

Share to Nitrate Reductase

Share to Periplasm

Share to Rhodobacter sphaeroides

Share to Solutions

Share to Spectrum Analysis

Source

Identifiers

PMID: 20146468
DOI: 10.1021/bi902140e

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-20146468-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Dependence of catalytic activity on driving force in solution assays and protein film voltammetry: insights from the comparison of nitrate reductase mutants.PMID 20146468Read ↗

Major Mo(V) EPR signature of Rhodobacter sphaeroides periplasmic nitrate reductase arising from a dead-end species that activates upon reduction. Relation to other molybdoenzymes from the DMSO reductase family.Semantic proximity Read ↗

Short circuiting a sulfite oxidising enzyme with direct electrochemistry: active site substitutions and their effect on catalysis and electron transfer.Semantic proximity Read ↗

Redox properties of wild-type and heme-binding loop mutants of bacterial cytochromes C measured by direct electrochemistry.Semantic proximity Read ↗

Investigating the function of [2Fe-2S] cluster N1a, the off-pathway cluster in complex I, by manipulating its reduction potential.Semantic proximity Read ↗

Geobacter sulfurreducens cytochrome c peroxidases: electrochemical classification of catalytic mechanisms.Semantic proximity Read ↗

Thin film voltammetry of wild type and mutant reaction center proteins from photosynthetic bacteria.Semantic proximity Read ↗

Modifications of protein environment of the [2Fe-2S] cluster of the bc1 complex: effects on the biophysical properties of the rieske iron-sulfur protein and on the kinetics of the complex.Semantic proximity Read ↗

Access to the active site of periplasmic nitrate reductase: insights from site-directed mutagenesis and zinc inhibition studies.Semantic proximity Read ↗

Design of fast enzymes by optimizing interaction potential in active site.Semantic proximity Read ↗

Design of a single protein that spans the entire 2-V range of physiological redox potentials.Semantic proximity Read ↗

Electrochemical characterization of mutant forms of rubredoxin B from Mycobacterium tuberculosis.Semantic proximity Read ↗

Experimental approaches to kinetics of gas diffusion in hydrogenase.Semantic proximity Read ↗

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