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Article

Ultrafast structural dynamics in BLUF domains: transient infrared spectroscopy of AppA and its mutants.

Journal of the American Chemical Society - 19 Dec 2007

Stelling Allison L, Ronayne Kate L, Nappa Jérôme, Tonge Peter J, Meech Stephen R

Abstract excerpt

The structural dynamics following photoexcitation of a photosensing BLUF (blue light sensing using FAD) domain protein have been investigated by ultrafast transient infrared spectroscopy. Specifically, the transcriptional antirepressor AppA from Rhodobacter sphaeroides has been studied in the light and dark adapted forms and in photoactive and inactive mutants W104F and Q63L. A transient absorption has been...

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Identifiers

PMID: 18031038
DOI: 10.1021/ja074074n

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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

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Ultrafast structural dynamics in BLUF domains: transient infrared spectroscopy of AppA and its mutants.PMID 18031038Read ↗

A Q63E Rhodobacter sphaeroides AppA BLUF domain mutant is locked in a pseudo-light-excited signaling state.Semantic proximity Read ↗

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The critical role of a hydrogen bond between Gln63 and Trp104 in the blue-light sensing BLUF domain that controls AppA activity.Semantic proximity Read ↗

Crystal structures of the AppA BLUF domain photoreceptor provide insights into blue light-mediated signal transduction.Semantic proximity Read ↗

Tryptophan at position 104 is involved in transforming light signal into changes of beta-sheet structure for the signaling state in the BLUF domain of AppA.Semantic proximity Read ↗

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