Department of Chemistry, University of Florida, Gainesville, FL 32611, USA.
Department of Chemistry, Boston College, Chestnut Hill, MA 02467, USA.
Acta Crystallogr D Struct Biol. 2017 Jul 1;73(Pt 7):573-580. doi: 10.1107/S2059798317007045. Epub 2017 Jun 30.
The enzyme DpgC is included in the small family of cofactor-independent dioxygenases. The chemistry of DpgC is uncommon as the protein binds and utilizes dioxygen without the aid of a metal or organic cofactor. Previous structural and biochemical studies identified the substrate-binding mode and the components of the active site that are important in the catalytic mechanism. In addition, the results delineated a putative binding pocket and migration pathway for the co-substrate dioxygen. Here, structural biology is utilized, along with site-directed mutagenesis, to probe the assigned dioxygen-binding pocket. The key residues implicated in dioxygen trafficking were studied to probe the process of binding, activation and chemistry. The results support the proposed chemistry and provide insight into the general mechanism of dioxygen binding and activation.
酶 DpgC 属于辅酶非依赖型双加氧酶的小家族。DpgC 的化学性质很不寻常，因为该蛋白在没有金属或有机辅因子的帮助下结合并利用了氧气。先前的结构和生化研究确定了底物结合模式和催化机制中重要的活性位点成分。此外，结果还描绘了辅底物氧气的假定结合口袋和迁移途径。在这里，结构生物学与定点突变一起被用来探测指定的氧气结合口袋。对涉及氧气运输的关键残基进行了研究，以探究结合、激活和化学过程。结果支持了所提出的化学，并深入了解了氧气结合和激活的一般机制。
