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

Palladium(II) and platinum(II) bind strongly to an engineered blue copper protein.

Inorganic chemistry - 21 Nov 2011

McLaughlin Matthew P, Darrah Thomas H, Holland Patrick L

Abstract excerpt

Studies of palladium(II) and platinum(II) binding to well-characterized proteins contribute to understanding the influence of these metals in the environment and body. The well-characterized apoprotein of azurin has a soft-metal binding site that may be exposed to solvent by mutation of a coordinating His-117 residue to glycine (H117G). Palladium(II) and platinum(II) form strong 1:1 adducts with the apo form of...

Read the complete abstract on PubMed

Topics

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

Share to Apoproteins
Share to Binding Sites
Share to Copper

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

Share to Models, Molecular

Share to Platinum

Share to Protein Conformation

Share to Protein Engineering

Share to Pseudomonas aeruginosa

Source

Open in PubMed Open full text

Identifiers

PMID: 22026434
DOI: 10.1021/ic2017648
PMCID: PMC3217333

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

Palladium(II) and platinum(II) bind strongly to an engineered blue copper protein.PMID 22026434Read ↗

Transforming a blue copper into a red copper protein: engineering cysteine and homocysteine into the axial position of azurin using site-directed mutagenesis and expressed protein ligation.Semantic proximity Read ↗

Redesigning the blue copper azurin into a redox-active mononuclear nonheme iron protein: preparation and study of Fe(II)-M121E azurin.Semantic proximity Read ↗

The structural role of the copper-coordinating and surface-exposed histidine residue in the blue copper protein azurin.Semantic proximity Read ↗

Copper-sulfenate complex from oxidation of a cavity mutant of Pseudomonas aeruginosa azurin.Semantic proximity Read ↗

Structural basis for organism-dependent effects on spectroscopic properties of type 1 copper azurin by the same axial methionine to histidine mutation.Semantic proximity Read ↗

Structural Basis for the Effects of Phenylalanine on Tuning the Reduction Potential of Type 1 Copper in Azurin.Semantic proximity Read ↗

Reduction potential variations in azurin through secondary coordination sphere phenylalanine incorporations.Semantic proximity Read ↗

Dimerization of a His117Gly azurin mutant by external addition of 1,omega-di(imidazol-1-yl)alkanes.Semantic proximity Read ↗

Design of a single protein that spans the entire 2-V range of physiological redox potentials.Semantic proximity Read ↗

Spectroscopic and mechanistic studies of type-1 and type-2 copper sites in Pseudomonas aeruginosa azurin as obtained by addition of external ligands to mutant His46Gly.Semantic proximity Read ↗

Role and oxidation state of the pterin molybdenum cofactor of molybdenum enzymes: studies of a Drosophila melanogaster xanthine dehydrogenase (rosy) variant, G1011E.Semantic proximity Read ↗

Disruption of the disulfide bridge in azurin from Pseudomonas aeruginosa.Semantic proximity Read ↗

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