Structural change of a cofactor binding site of flavoprotein detected by single-protein fluorescence spectroscopy at 1.5 k

The visible fluorescence spectrum of single flavoprotein at a temperature of 1.5 K has been measured by one-photon excitation. The flavoprotein studied was a photoswitchable enzyme, photoactivated adenylyl cyclase. The time course of the spectrum revealed a structural change occurring at a rate of 1...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	Physical review letters 2011-02, Vol.106 (7), p.078101-078101, Article 078101
Hauptverfasser:	Fujiyoshi, Satoru, Hirano, Mitsuharu, Matsushita, Michio, Iseki, Mineo, Watanabe, Masakatsu
Format:	Artikel
Sprache:	eng
Schlagworte:	Binding Sites BOSONS CLASSICAL AND QUANTUM MECHANICS, GENERAL PHYSICS ELEMENTARY PARTICLES ELEMENTS EMISSION SPECTROSCOPY ENERGY-LEVEL TRANSITIONS Euglena gracilis EXCITATION Flavins - metabolism Flavoproteins - chemistry Flavoproteins - metabolism FLUORESCENCE SPECTROSCOPY HETEROCYCLIC COMPOUNDS HYDROGEN Hydrogen Bonding INORGANIC, ORGANIC, PHYSICAL AND ANALYTICAL CHEMISTRY ISOALLOXAZINES MASSLESS PARTICLES Models, Molecular NONMETALS ORGANIC COMPOUNDS ORGANIC NITROGEN COMPOUNDS ORGANIC OXYGEN COMPOUNDS PHOTONS Protein Structure, Tertiary PROTEINS Protozoan Proteins - chemistry Protozoan Proteins - metabolism SPECTRA Spectrometry, Fluorescence - methods SPECTROSCOPY Temperature TEMPERATURE RANGE TEMPERATURE RANGE 0000-0013 K
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Beschreibung
Zusammenfassung:	The visible fluorescence spectrum of single flavoprotein at a temperature of 1.5 K has been measured by one-photon excitation. The flavoprotein studied was a photoswitchable enzyme, photoactivated adenylyl cyclase. The time course of the spectrum revealed a structural change occurring at a rate of 10(-3) s(-1) around hydrogen bonds at the flavin cofactor binding site.
ISSN:	0031-9007 1079-7114
DOI:	10.1103/physrevlett.106.078101