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

The Met80Ala and Tyr67His/Met80Ala mutants of human cytochrome c shed light on the reciprocal role of Met80 and Tyr67 in regulating ligand access into the heme pocket.

Journal of inorganic biochemistry - 1 Apr 2017

Ciaccio Chiara, Tognaccini Lorenzo, Battista Theo, Cervelli Manuela, Howes Barry D, Santucci Roberto, Coletta Massimo, Mariottini Paolo, Smulevich Giulietta, Fiorucci Laura

Abstract excerpt

The spectroscopic and functional properties of the single Met80Ala and double Tyr67His/Met80Ala mutants of human cytochrome c have been investigated in their ferric and ferrous forms, and in the presence of different ligands, in order to clarify the reciprocal effect of these two residues in regulating the access of exogenous molecules into the heme pocket. In the ferric state, both mutants display an aquo high...

Read the complete abstract on PubMed

Topics

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

Share to Alanine
Share to Circular Dichroism

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

Share to Cytochromes c

Share to Histamine

Share to Methionine

Share to Structure-Activity Relationship

Share to Tyrosine

Source

Identifiers

PMID: 28161681
DOI: 10.1016/j.jinorgbio.2017.01.008

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The Met80Ala and Tyr67His/Met80Ala mutants of human cytochrome c shed light on the reciprocal role of Met80 and Tyr67 in regulating ligand access into the heme pocket.PMID 28161681Read ↗

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 ↗

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

Protein stability and mutations in the axial methionine loop of a minimal cytochrome c.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 ↗

Yeast iso-1-cytochrome c met80X mutants: the pKa of the spin state transition as a probe for haem pocket flexibility.Semantic proximity Read ↗

The proportion of Met80-sulfoxide dictates 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 ↗

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

Perturbation of the redox site structure of cytochrome c variants upon tyrosine nitration.Semantic proximity Read ↗

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

Structural and functional characterization of phosphomimetic mutants of cytochrome c at threonine 28 and serine 47.Semantic proximity Read ↗

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