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

Effects of the protein environment on the spectral properties of tryptophan radicals in Pseudomonas aeruginosa azurin.

Journal of the American Chemical Society - 27 Mar 2013

Bernini Caterina, Andruniów Tadeusz, Olivucci Massimo, Pogni Rebecca, Basosi Riccardo, Sinicropi Adalgisa

Abstract excerpt

Many biological electron-transfer reactions involve short-lived tryptophan radicals as key reactive intermediates. While these species are difficult to investigate, the recent photogeneration of a long-lived neutral tryptophan radical in two Pseudomonas aeruginosa azurin mutants (Az48W and ReAz108W) made it possible to characterize the electronic, vibrational, and magnetic properties of such species and their...

Read the complete abstract on PubMed

Topics

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

Share to Electron Spin Resonance Spectroscopy
Share to Hydrogen Bonding

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Protein Conformation

Share to Pseudomonas aeruginosa

Share to Quantum Theory

Share to Spectrophotometry, Ultraviolet

Share to Spectrum Analysis, Raman

Share to Tryptophan

Source

Identifiers

PMID: 23458492
DOI: 10.1021/ja400464n

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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

Effects of the protein environment on the spectral properties of tryptophan radicals in Pseudomonas aeruginosa azurin.PMID 23458492Read ↗

Spectroscopic comparison of photogenerated tryptophan radicals in azurin: effects of local environment and structure.Semantic proximity Read ↗

Charge delocalization in the special-pair radical cation of mutant reaction centers of Rhodobacter sphaeroides from Stark spectra and nonadiabatic spectral simulations.Semantic proximity Read ↗

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

EPR parameters of amino acid radicals in P. eryngii versatile peroxidase and its W164Y variant computed at the QM/MM level.Semantic proximity Read ↗

Photogeneration and Quenching of Tryptophan Radical in Azurin.Semantic proximity Read ↗

Effect of lysine ionization on the structure and electrochemical behaviour of the Met44-->Lys mutant of the blue-copper protein azurin from Pseudomonas aeruginosa.Semantic proximity Read ↗

Conformationally Dynamic Radical Transfer within Ribonucleotide Reductase.Semantic proximity Read ↗

Mutations in transhydrogenase change the fluorescence emission state of TRP72 from 1La to 1Lb.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 ↗

The stacking tryptophan of galactose oxidase: a second-coordination sphere residue that has profound effects on tyrosyl radical behavior and enzyme catalysis.Semantic proximity Read ↗

Quantum chemical modeling of rhodopsin mutants displaying switchable colors.Semantic proximity Read ↗

Ab initio and QM/MM study of electron addition on the disulfide bond in thioredoxin.Semantic proximity Read ↗

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