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-dependent stability, protonation, and reactivity of cysteine-bound heme proteins.

Proceedings of the National Academy of Sciences of the United States of America - 21 Jan 2014

Zhong Fangfang, Lisi George P, Collins Daniel P, Dawson John H, Pletneva Ekaterina V

Abstract excerpt

Cysteine-bound hemes are key components of many enzymes and biological sensors. Protonation (deprotonation) of the Cys ligand often accompanies redox transformations of these centers. To characterize these phenomena, we have engineered a series of Thr78Cys/Lys79Gly/Met80X mutants of yeast cytochrome c (cyt c) in which Cys78 becomes one of the axial ligands to the heme. At neutral pH, the protonation state of the...

Read the complete abstract on PubMed

Topics

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

Share to Cytochromes c
Share to Electron Transport

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

Share to Hemeproteins

Share to Horses

Share to Peroxidases

Share to Spectrophotometry

Share to Sulfhydryl Compounds

Source

Open in PubMed Open full text

Identifiers

PMID: 24398520
DOI: 10.1073/pnas.1317173111
PMCID: PMC3903235

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

Redox-dependent stability, protonation, and reactivity of cysteine-bound heme proteins.PMID 24398520Read ↗

Distal Unfolding of Ferricytochrome c Induced by the F82K Mutation.Semantic proximity Read ↗

Elucidating the role of the proximal cysteine hydrogen-bonding network in ferric cytochrome P450cam and corresponding mutants using magnetic circular dichroism spectroscopy.Semantic proximity Read ↗

Dynamics of the His79-heme alkaline transition of yeast iso-1-cytochrome c probed by conformationally gated electron transfer with Co(II)bis(terpyridine).Semantic proximity Read ↗

Mutation of Pro76 affects the dynamics of Ω-loop D of yeast Iso-1-cytochrome c: Application of gated electron transfer.Semantic proximity Read ↗

Distinct roles of a tyrosine-associated hydrogen-bond network in fine-tuning the structure and function of heme proteins: two cases designed for myoglobin.Semantic proximity Read ↗

Effect of a K72A Mutation on the Structure, Stability, Dynamics, and Peroxidase Activity of Human Cytochrome c.Semantic proximity Read ↗

Structure, Function and Dynamics of mCoral, a pH-Responsive Engineered Variant of the mCherry Fluorescent Protein with Improved Hydrogen Peroxide Tolerance.Semantic proximity Read ↗

Heme-iron ligand (M80-Fe) in cytochrome c is destabilizing: combined in vitro and in silico approaches to monitor changes in structure, stability and dynamics of the protein on mutation.Semantic proximity Read ↗

Structural characteristics of the redox-sensing coiled coil in the voltage-gated H+ channel.Semantic proximity Read ↗

Molecular insights on the conformational dynamics of a P76C mutant of human cytochrome c and the enhancement on its peroxidase activity.Semantic proximity Read ↗

Key Structural Motifs Balance Metal Binding and Oxidative Reactivity in a Heterobimetallic Mn/Fe Protein.Semantic proximity Read ↗

Mechanistic insights into the superoxide-cytochrome c reaction by lysine surface scanning.Semantic proximity Read ↗

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