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

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.

Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry - 1 Jun 2001

Xiao Z, Gardner A R, Cross M, Maes E M, Czernuszewicz R S, Sola M, Wedd A G

Abstract excerpt

Redox thermodynamic data provide a detailed insight into control of the reduction potential E degrees' of the [Fe(S-Cys)4] site in rubredoxin. Mutant forms were studied in which specific structural changes were made in both the primary and secondary coordination spheres. Those changes have been probed by resonance Raman spectroscopy. The decrease of approximately 200 mV in E degrees' observed for the...

Read the complete abstract on PubMed

Topics

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

Share to Clostridium
Share to Cysteine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Models, Molecular

Share to Oxidation-Reduction

Share to Protein Conformation

Share to Recombinant Proteins

Share to Serine

Share to Thermodynamics

Source

Identifiers

PMID: 11472027
DOI: 10.1007/s007750100241

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

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.PMID 11472027Read ↗

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

Conformation, stability, and active-site cysteine titrations of Escherichia coli D26A thioredoxin probed by Raman spectroscopy.Semantic proximity Read ↗

Structural and denaturation studies of two mutants of a cold adapted superoxide dismutase point to the importance of electrostatic interactions in protein stability.Semantic proximity Read ↗

Hydrogen bonding to the cysteine ligand of superoxide reductase: acid-base control of the reaction intermediates.Semantic proximity Read ↗

Changes in hydrogen-bond strengths explain reduction potentials in 10 rubredoxin variants.Semantic proximity Read ↗

Structural and functional characterization of the unusual triheme cytochrome bound to the reaction center of Rhodovulum sulfidophilum.Semantic proximity Read ↗

Redox-dependent stability, protonation, and reactivity of cysteine-bound heme proteins.Semantic proximity Read ↗

Anatomy of a red copper center: spectroscopic identification and reactivity of the copper centers of Bacillus subtilis Sco and its Cys-to-Ala variants.Semantic proximity Read ↗

Proton-assisted two-electron transfer in natural variants of tetraheme cytochromes from Desulfomicrobium Sp.Semantic proximity Read ↗

Crystallographic studies of V44 mutants of Clostridium pasteurianum rubredoxin: effects of side-chain size on reduction potential.Semantic proximity Read ↗

A pure S = 3/2 [Fe4S4]+ cluster in the A33Y variant of Pyrococcus furiosus ferredoxin.Semantic proximity Read ↗

Ultrahigh-resolution study on Pyrococcus abyssi rubredoxin: II. Introduction of an O-H...Sgamma-Fe hydrogen bond increased the reduction potential by 65 mV.Semantic proximity Read ↗

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