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

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

Journal of inorganic biochemistry - 1 Jul 2026

Bandi Swati, Bowler Bruce E

Abstract excerpt

Cytochrome c (Cytc) contains two Ω-loops (C, residues 40-57 and D, residues 70-85) that control access of Cytc to alternate conformers needed to convert it from an electron transfer (ET) protein to an enzyme with peroxidase activity. As a peroxidase, Cytc oxygenates the mitochondrial lipid cardiolipin, which is an early signal in apoptosis. We probe the role of Pro76, a highly conserved residue in Ω-loop D, in...

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
Share to Hydrogen-Ion Concentration

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

Share to Mutation

Share to Proline

Share to Saccharomyces cerevisiae

Share to Saccharomyces cerevisiae Proteins

Source

Identifiers

PMID: 41812586
DOI: 10.1016/j.jinorgbio.2026.113296

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 16 Oct 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

Mutation of Pro76 affects the dynamics of Ω-loop D of yeast Iso-1-cytochrome c: Application of gated electron transfer.PMID 41812586Read ↗

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

Probing the dynamics of a His73-heme alkaline transition in a destabilized variant of yeast iso-1-cytochrome c with conformationally gated electron transfer methods.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 ↗

Binding of S. cerevisiae iso-1 cytochrome c and its surface lysine-to-alanine variants to cardiolipin: charge effects and the role of the lipid to protein ratio.Semantic proximity Read ↗

Influence of cysteine-directed mutations at the Ω-loops on peroxidase activity of human cytochrome c.Semantic proximity Read ↗

Probing the bottom of a folding funnel using conformationally gated electron transfer reactions.Semantic proximity Read ↗

The Increase in the Peroxidase Activity of the Cytochrome C with Substitutions in the Universal Binding Site Is Associated with Changes in the Ability to Interact with External Ligands.Semantic proximity Read ↗

Differences in functional cross-talk between loops C and D in two mitochondrial cytochromes.Semantic proximity Read ↗

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

Tyrosine phosphorylation turns alkaline transition into a biologically relevant process and makes human cytochrome c behave as an anti-apoptotic switch.Semantic proximity Read ↗

Site A-Mediated Partial Unfolding of Cytochrome c on Cardiolipin Vesicles Is Species-Dependent and Does Not Require Lys72.Semantic proximity Read ↗

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

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