The Crystal Structure of Cytochrome P450 4B1 (CYP4B1) Monooxygenase Complexed with Octane Discloses Several Structural Adaptations for ω-Hydroxylation

P450 family 4 fatty acid ω-hydroxylases preferentially oxygenate primary C–H bonds over adjacent, energetically favored secondary C–H bonds, but the mechanism explaining this intriguing preference is unclear. To this end, the structure of rabbit P450 4B1 complexed with its substrate octane was deter...

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Veröffentlicht in:	The Journal of biological chemistry 2017-03, Vol.292 (13), p.5610-5621
Hauptverfasser:	Hsu, Mei-Hui, Baer, Brian R., Rettie, Allan E., Johnson, Eric F.
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Aryl Hydrocarbon Hydroxylases - chemistry Binding Sites Conserved Sequence Crystallography, X-Ray cytochrome P450 Editors' Picks enzyme structure fatty acid metabolism heme Heme - chemistry Heme - metabolism Hydroxylation membrane protein Octanes - chemistry Protein Conformation Rabbits Structure-Activity Relationship Substrate Specificity X-ray crystallography xenobiotic
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