Ultrafast infrared spectroscopy reveals water-mediated coherent dynamics in an enzyme active site.

ABSTRACT: Understanding the impact of fast dynamics upon the chemical processes occurring within the active sites of proteins and enzymes is a key challenge that continues to attract significant interest, though direct experimental insight in the solution phase remains sparse. Similar gaps in our knowledge exist in understanding the role played by water, either as a solvent or as a structural/dynamic component of the active site. In order to investigate further the potential biological roles of water, we have employed ultrafast multidimensional infrared spectroscopy experiments that directly probe the structural and vibrational dynamics of NO bound to the ferric haem of the catalase enzyme from Corynebacterium glutamicum in both H₂O and D₂O. Despite catalases having what

SUBMITTER: Adamczyk K 

PROVIDER: S-EPMC5588449 | biostudies-literature | 2015 Jan

REPOSITORIES: biostudies-literature