Probing the NADH- and Methyl Red-binding site of a FMN-dependent azoreductase (AzoA) from Enterococcus faecalis

► A synergetic strategy was used to investigate the binding of NADH and Methyl Red in AzoA. ► Methyl Red and NADH lay against the flavin isoalloxazine ring at an angle of 45° and 35°. ► There were 12 and 19 amino acid residues participated in the binding of Methyl Red and NADH. ► Functional perturba...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	Archives of biochemistry and biophysics 2012-04, Vol.520 (2), p.99-107
Hauptverfasser:	Feng, Jinhui, Kweon, Ohgew, Xu, Haiyan, Cerniglia, Carl E., Chen, Huizhong
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenine Amino acids Azo Compounds - chemistry Azo dye azo dyes Azoreductase Benzoic acid Binding Sites Computer applications Enterococcus faecalis Enterococcus faecalis - enzymology Enzyme Activation Flavin mononucleotide Flavin Mononucleotide - chemistry Molecular Probe Techniques Mutation NAD (coenzyme) NAD - chemistry NADH NADH, NADPH Oxidoreductases - chemistry nicotinamide prediction Protein Binding Ribose Site-directed mutagenesis
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Schreiben Sie den ersten Kommentar!