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

Thermodynamic aspects of the adsorption of cytochrome c and its mutants on kaolinite.

Langmuir : the ACS journal of surfaces and colloids - 16 Jun 2009

Castellini Elena, Ranieri Antonio, Simari Domenico A, Di Rocco Giulia

Abstract excerpt

The adsorption of native, wild-type, and engineered cytochrome c on sodium-exchanged kaolinite was investigated by spectroscopic means. The variants of yeast cytochrome c were obtained replacing surface lysines in positions 72, 73, and 79 with alanine residues. All proteins are strongly adsorbed onto kaolinite. In particular, the presence of the lysine residue in position 73 remarkably favors adsorption. A...

Read the complete abstract on PubMed

Topics

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

Share to Adsorption
Share to Biocatalysis
Share to Cytochromes c

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

Share to Models, Molecular

Share to Mutation

Share to Spectrophotometry, Ultraviolet

Share to Thermodynamics

Source

Identifiers

PMID: 19425602
DOI: 10.1021/la9001016

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

Thermodynamic aspects of the adsorption of cytochrome c and its mutants on kaolinite.PMID 19425602Read ↗

pH-Dependent peroxidase activity of yeast cytochrome c and its triple mutant adsorbed on kaolinite.Semantic proximity Read ↗

Cytochrome c/cytochrome c peroxidase complex: effect of binding-site mutations on the thermodynamics of complex formation.Semantic proximity Read ↗

Differential adsorption of variants of the Thermomyces lanuginosus lipase on a hydrophobic surface suggests a role for local flexibility.Semantic proximity Read ↗

Disentangling electron tunneling and protein dynamics of cytochrome c through a rationally designed surface mutation.Semantic proximity Read ↗

Microcalorimetric characterization of the anion-exchange adsorption of recombinant cytochrome b5 and its surface-charge mutants.Semantic proximity Read ↗

The structural and functional role of lysine residues in the binding domain of cytochrome c in the electron transfer to cytochrome c oxidase.Semantic proximity Read ↗

Free energy of transition for the individual alkaline conformers of yeast iso-1-cytochrome c.Semantic proximity Read ↗

Cytochrome C on a gold surface: investigating structural relaxations and their role in protein-surface electron transfer by molecular dynamics simulations.Semantic proximity Read ↗

Cytochrome-c-binding site on cytochrome oxidase in Paracoccus denitrificans.Semantic proximity Read ↗

Protein adsorption orientation in the light of fluorescent probes: mapping of the interaction between site-directly labeled human carbonic anhydrase II and silica nanoparticles.Semantic proximity Read ↗

Thermodynamics of hydrogen cyanide and hydrogen fluoride binding to cytochrome c peroxidase and its Asn-82-->Asp mutant.Semantic proximity Read ↗

Cu(II)-binding properties of a cytochrome c with a synthetic metal-binding site: His-X3-His in an alpha-helix.Semantic proximity Read ↗

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