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

Kinetic isotope effect studies on the de novo rate of chromophore formation in fast- and slow-maturing GFP variants.

Biochemistry - 23 Sept 2008

Pouwels Lauren J, Zhang Liping, Chan Nam H, Dorrestein Pieter C, Wachter Rebekka M

Abstract excerpt

The maturation process of green fluorescent protein (GFP) entails a protein oxidation reaction triggered by spontaneous backbone condensation. The chromophore is generated by full conjugation of the Tyr66 phenolic group with the heterocycle, a process that requires C-H bond scission at the benzylic carbon. We have prepared isotope-enriched protein bearing tyrosine residues deuterated at the beta carbon, and have...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Substitution
Share to Deuterium Exchange Measurement

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Green Fluorescent Proteins

Share to Kinetics

Share to Oxidation-Reduction

Share to Solubility

Share to Spectrometry, Mass, Electrospray Ionization

Share to Tyrosine

Source

Open in PubMed Open full text

Identifiers

PMID: 18759496
DOI: 10.1021/bi8007164
PMCID: PMC2643082

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

Kinetic isotope effect studies on the de novo rate of chromophore formation in fast- and slow-maturing GFP variants.PMID 18759496Read ↗

Mechanism and energetics of green fluorescent protein chromophore synthesis revealed by trapped intermediate structures.Semantic proximity Read ↗

The crystal structure of the Y66L variant of green fluorescent protein supports a cyclization-oxidation-dehydration mechanism for chromophore maturation.Semantic proximity Read ↗

Uncovering the hidden ground state of green fluorescent protein.Semantic proximity Read ↗

Two independent routes of post-translational chemistry in fluorescent protein FusionRed.Semantic proximity Read ↗

Structure-guided engineering of a fast genetically encoded sensor for real-time H <sub>2</sub> O <sub>2</sub> monitoringSemantic proximity Read ↗

Common pathway for the red chromophore formation in fluorescent proteins and chromoproteins.Semantic proximity Read ↗

Ultra-fast genetically encoded sensor for precise real-time monitoring of physiological and pathophysiological peroxide dynamicsSemantic proximity Read ↗

Kinetic isotope effects on the noncovalent flavin mutant protein of pyranose 2-oxidase reveal insights into the flavin reduction mechanism.Semantic proximity Read ↗

Photophysics of EGFP (E222H) Mutant, with Comparisons to Model Chromophores: Excited State pK's, Progressions, Quenching and Exciton Interaction.Semantic proximity Read ↗

Kinetic and vibrational isotope effects of proton transfer reactions in channelrhodopsin-2.Semantic proximity Read ↗

Chromophore formation in DsRed occurs by a branched pathway.Semantic proximity Read ↗

Genetic Code Expansion Tools to Study Lysine AcylationSemantic proximity Read ↗

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