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

Role of Gln1029 in the photoactivation processes of the LOV2 domain in adiantum phytochrome3.

Biochemistry - 6 Jul 2004

Nozaki Dai, Iwata Tatsuya, Ishikawa Tomoko, Todo Takeshi, Tokutomi Satoru, Kandori Hideki

Abstract excerpt

Phototropin (phot) is a blue-light receptor in plants. The molecule has two FMN (flavin mononucleotide)-binding domains named the LOV (light-oxygen-voltage) domain, that is a subset of a PAS (per-arnt-sim) superfamily. Illumination of phot-LOV domains produces a covalent C(4a) flavin-cysteinyl adduct, which is called the S390 intermediate state. According to the crystal structures of the LOV2 domain of Adiantum...

Read the complete abstract on PubMed

Topics

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

Share to Crystallography, X-Ray
Share to Glutamine
Share to Hydrogen Bonding

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Oxygen

Share to Phytochrome

Share to Spectroscopy, Fourier Transform Infrared

Share to Ultraviolet Rays

Source

Identifiers

PMID: 15222749
DOI: 10.1021/bi0494727

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Role of Gln1029 in the photoactivation processes of the LOV2 domain in adiantum phytochrome3.PMID 15222749Read ↗

Light signal transduction pathway from flavin chromophore to the J alpha helix of Arabidopsis phototropin1.Semantic proximity Read ↗

Transient IR spectroscopy identifies key interactions and unravels new intermediates in the photocycle of a bacterial phytochrome.Semantic proximity Read ↗

Time-resolved Fourier transform infrared study on photoadduct formation and secondary structural changes within the phototropin LOV domain.Semantic proximity Read ↗

The photocycle of a flavin-binding domain of the blue light photoreceptor phototropin.Semantic proximity Read ↗

Local Electric Field Changes during the Photoconversion of the Bathy Phytochrome Agp2.Semantic proximity Read ↗

Phototropin LOV domains exhibit distinct roles in regulating photoreceptor function.Semantic proximity Read ↗

NDPK2 as a signal transducer in the phytochrome-mediated light signaling.Semantic proximity Read ↗

Irreversible photoreduction of flavin in a mutated Phot-LOV1 domain.Semantic proximity Read ↗

A conserved isoleucine in the LOV1 domain of a novel phototropin from the marine alga Ostreococcus tauri modulates the dark state recovery of the domain.Semantic proximity Read ↗

Probing the allostery in dimeric near-infrared biomarkers derived from the bacterial phytochromes: The impact of the T204A substitution on the inter-monomer interaction.Semantic proximity Read ↗

Diverse roles of glycine residues conserved in photoactive yellow proteins.Semantic proximity Read ↗

Unusual photodynamic characteristics of the light-oxygen-voltage domain of phototropin linked to terrestrial adaptation of Klebsormidium nitens.Semantic proximity Read ↗

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