Controlling Conformational Flexibility of an O2-Binding H-NOX Domain

Heme Nitric oxide/OXygen binding (H-NOX) domains have provided a novel scaffold to probe ligand affinity in hemoproteins. Mutation of isoleucine 5, a conserved residue located in the heme-binding pocket of the H-NOX domain from Thermoanaerobacter tengcongensis (Tt H-NOX), was carried out to examine...

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Veröffentlicht in:	Biochemistry (Easton) 2011-08, Vol.50 (32), p.6832-6840
Hauptverfasser:	Weinert, Emily E, Phillips-Piro, Christine M, Tran, Rosalie, Mathies, Richard A, Marletta, Michael A
Format:	Artikel
Sprache:	eng
Schlagworte:	Crystallography, X-Ray Hemeproteins - chemistry Hemeproteins - metabolism Models, Molecular Nitric Oxide - chemistry Nitric Oxide - metabolism Oxygen - metabolism Protein Conformation Spectrophotometry, Ultraviolet Spectrum Analysis, Raman Thermoanaerobacter - metabolism
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