3-Fluorotyrosine as a complementary probe of hemoglobin structure and dynamics: a (19)F-NMR study of Synechococcus sp. PCC 7002 GlbN

The hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002 (GlbN) contains three tyrosines (Tyr5, Tyr22, and Tyr53), each of which undergoes a structural rearrangement when the protein binds an exogenous ligand such as cyanide. We explored the use of 3-fluorotyrosine and (19)F-NMR spectroscop...

Ausführliche Beschreibung

Bibliographische Detailangaben

Veröffentlicht in:	Chemistry & biodiversity 2012-09, Vol.9 (9), p.1703-1717
Hauptverfasser:	Pond, Matthew P, Wenke, Belinda B, Preimesberger, Matthew R, Rice, Selena L, Lecomte, Juliette T J
Format:	Artikel
Sprache:	eng
Schlagworte:	Bacterial Proteins - chemistry Bacterial Proteins - metabolism Hemoglobins - chemistry Hemoglobins - metabolism Magnetic Resonance Spectroscopy Models, Molecular Synechococcus - chemistry Synechococcus - metabolism Truncated Hemoglobins - chemistry Truncated Hemoglobins - metabolism Tyrosine - analogs & derivatives Tyrosine - chemistry
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!