Xanthine oxidase-product complexes probe the importance of substrate/product orientation along the reaction coordinate.

ABSTRACT: A combination of reaction coordinate computations, resonance Raman spectroscopy, spectroscopic computations, and hydrogen bonding investigations have been used to understand the importance of substrate orientation along the xanthine oxidase reaction coordinate. Specifically, 4-thiolumazine and 2,4-dithiolumazine have been used as reducing substrates for xanthine oxidase to form stable enzyme-product charge transfer complexes suitable for spectroscopic study. Laser excitation into the near-infrared molybdenum-to-product charge transfer band produces rR enhancement patterns in the high frequency in-plane stretching region that directly probe the nature of this MLCT transition and provide insight into the effects of electron redistribution along the reaction coordinate between the transition

SUBMITTER: Yang J 

PROVIDER: S-EPMC5634921 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature