Oxygen diffusion pathways in a cofactor-independent dioxygenase.

ABSTRACT: Molecular oxygen plays an important role in a wide variety of enzymatic reactions. Through recent research efforts combining computational and experimental methods a new view of O₂ diffusion is emerging, where specific channels guide O₂ to the active site. The focus of this work is DpgC, a cofactor-independent oxygenase. Molecular dynamics simulations, together with mutagenesis experiments and xenon-binding data, reveal that O₂ reaches the active site of this enzyme using three main pathways and four different access points. These pathways connect a series of dynamic hydrophobic pockets, concentrating O₂ at a specific face of the enzyme substrate. Extensive molecular dynamics simulations provide information about which pathways are more frequentl

SUBMITTER: Di Russo NV 

PROVIDER: S-EPMC4618494 | biostudies-literature | 2015 Nov

REPOSITORIES: biostudies-literature