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

A role of methionine 100 in facilitating PYP(M)-decay process in the photocycle of photoactive yellow protein.

Journal of biochemistry - 1 Aug 2002

Kumauchi Masato, Hamada Norio, Sasaki Jun, Tokunaga Fumio

Abstract excerpt

PYP (photoactive yellow protein) is a photoreceptor protein, which is activated upon photo-isomerization of the p-coumaric acid chromophore and is inactivated as the chromophore is thermally back-isomerized within a second (in PYP(M)-to-PYP(dark) conversion). Here we have examined the mechanism of the rapid thermal isomerization by analyzing mutant PYPs of Met100, which was previously shown to play a major role...

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Proteins
Share to Darkness
Share to Isomerism

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Methionine

Share to Molecular Structure

Share to Statistics as Topic

Share to Temperature

Source

Identifiers

PMID: 12153716
DOI: 10.1093/oxfordjournals.jbchem.a003211

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

A role of methionine 100 in facilitating PYP(M)-decay process in the photocycle of photoactive yellow protein.PMID 12153716Read ↗

Regulation of Photocycle Kinetics of Photoactive Yellow Protein by Modulating Flexibility of the β-Turn.Semantic proximity Read ↗

Structural role of tyrosine 98 in photoactive yellow protein: effects on fluorescence, gateway, and photocycle recovery.Semantic proximity Read ↗

Mechanistic pathways for the photoisomerization reaction of the anchored, tethered chromophore of the photoactive yellow protein and its mutants.Semantic proximity Read ↗

Out of the blue: the photocycle of the photoactive yellow protein.Semantic proximity Read ↗

Influence of the crystalline state on photoinduced dynamics of photoactive yellow protein studied by ultraviolet-visible transient absorption spectroscopy.Semantic proximity Read ↗

Capturing the photo-signaling state of a photoreceptor in a steady-state fashion by binding a transition metal complex.Semantic proximity Read ↗

Influence of a chromophore analogue in the protein cage of a photoactive yellow protein.Semantic proximity Read ↗

Structural change of site-directed mutants of PYP: new dynamics during pR state.Semantic proximity Read ↗

Time-resolved single tryptophan fluorescence in photoactive yellow protein monitors changes in the chromophore structure during the photocycle via energy transfer.Semantic proximity Read ↗

Effect of salt and pH on the activation of photoactive yellow protein and gateway mutants Y98Q and Y98F.Semantic proximity Read ↗

Structural changes during the photocycle of photoactive yellow protein monitored by ultraviolet resonance raman spectra of tyrosine and tryptophan.Semantic proximity Read ↗

Photoionization and electron radical recombination dynamics in photoactive yellow protein investigated by ultrafast spectroscopy in the visible and near-infrared spectral region.Semantic proximity Read ↗

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