Crystal Structures of Cyclohexanone Monooxygenase Reveal Complex Domain Movements and a Sliding Cofactor

Cyclohexanone monooxygenase (CHMO) is a flavoprotein that carries out the archetypical Baeyer−Villiger oxidation of a variety of cyclic ketones into lactones. Using NADPH and O2 as cosubstrates, the enzyme inserts one atom of oxygen into the substrate in a complex catalytic mechanism that involves t...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	Journal of the American Chemical Society 2009-07, Vol.131 (25), p.8848-8854
Hauptverfasser:	Mirza, I. Ahmad, Yachnin, Brahm J, Wang, Shaozhao, Grosse, Stephan, Bergeron, Hélène, Imura, Akihiro, Iwaki, Hiroaki, Hasegawa, Yoshie, Lau, Peter C. K, Berghuis, Albert M
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence ARGININE ATOMS CRYSTAL STRUCTURE Crystallography, X-Ray CYCLOHEXANONE ENZYMES Flavin-Adenine Dinucleotide - chemistry Flavin-Adenine Dinucleotide - metabolism ISOALLOXAZINES KETONES LACTONES MATERIALS SCIENCE Models, Molecular NADP NADP - chemistry NADP - metabolism national synchrotron light source NICOTINAMIDE OXIDATION OXYGEN Oxygenases - chemistry Oxygenases - metabolism Protein Binding Protein Conformation Protein Structure, Tertiary PROTEINS RANGE RHODOCOCCUS Rhodococcus - enzymology SHAPE SIZE STRAINS Substrate Specificity SUBSTRATES TRYPTOPHAN
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Schreiben Sie den ersten Kommentar!