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

Control of reduction thermodynamics in [2Fe-2S] ferredoxins Entropy-enthalpy compensation and the influence of surface mutations.

Journal of inorganic biochemistry - 1 Jun 2010

Bellei Marzia, Battistuzzi Gianantonio, Wu Shu-pao, Mansy Sheref S, Cowan James A, Sola Marco

Abstract excerpt

The reaction thermodynamics for the one-electron reduction of the [2Fe-2S] cluster of both human ferredoxin and various surface point mutants, in which each of the negatively charged residues Asp72, Glu73, Asp76, and Asp79 were converted to Ala, have been determined by variable temperature spectroelectrochemical measurements. The above are conserved residues that have been implicated in interactions between the...

Read the complete abstract on PubMed

Topics

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

Share to Electrochemistry
Share to Entropy

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Ferredoxins

Share to Iron-Sulfur Proteins

Share to Models, Molecular

Share to Sequence Homology, Amino Acid

Share to Structure-Activity Relationship

Share to Thermodynamics

Source

Open in PubMed Open full text

Identifiers

PMID: 20362339
DOI: 10.1016/j.jinorgbio.2010.03.001
PMCID: PMC2891050

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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

Control of reduction thermodynamics in [2Fe-2S] ferredoxins Entropy-enthalpy compensation and the influence of surface mutations.PMID 20362339Read ↗

Redox reactivity of the heme Fe3+/Fe 2+ couple in native myoglobins and mutants with peroxidase-like activity.Semantic proximity Read ↗

Fold versus sequence effects on the driving force for protein-mediated electron transfer.Semantic proximity Read ↗

Effects of mutating aromatic surface residues of the heme domain of human sulfite oxidase on its heme midpoint potential, intramolecular electron transfer, and steady-state kinetics.Semantic proximity Read ↗

Redox thermodynamics of mutant forms of the rubredoxin from Clostridiumpasteurianum: identification of a stable Fe(III)(S-Cys)3(OH) centre in the C6S mutant.Semantic proximity Read ↗

Electrostatic interactions stabilizing ferredoxin electron transfer complexes. Disruption by "conservative" mutations.Semantic proximity Read ↗

Allostery in the ferredoxin protein motif does not involve a conformational switch.Semantic proximity Read ↗

Solvation effects on S K-edge XAS spectra of Fe-S proteins: normal and inverse effects on WT and mutant rubredoxin.Semantic proximity Read ↗

Biochemical and Biophysical Methods to Examine the Effects of Site-Directed Mutagenesis on Enzymatic Activities and Interprotein Interactions.Semantic proximity Read ↗

Atomic resolution structures of rieske iron-sulfur protein: role of hydrogen bonds in tuning the redox potential of iron-sulfur clusters.Semantic proximity Read ↗

Investigation of the role of surface residues in the ferredoxin from Clostridium pasteurianum.Semantic proximity Read ↗

Calorimetric studies of the N-terminal half-molecule of transferrin and mutant forms modified near the Fe(3+)-binding site.Semantic proximity Read ↗

NMR study of the electron transfer complex of plant ferredoxin and sulfite reductase: mapping the interaction sites of ferredoxin.Semantic proximity Read ↗

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