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Correlating CH Bond Cleavage with Molybdenum Reduction in Xanthine Oxidase
Author(s) -
Kirk Martin L.,
Berhane Abebe
Publication year - 2012
Publication title -
chemistry and biodiversity
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.427
H-Index - 70
eISSN - 1612-1880
pISSN - 1612-1872
DOI - 10.1002/cbdv.201200073
Subject(s) - chemistry , bond cleavage , molybdenum , xanthine oxidase , reaction coordinate , acceptor , stereochemistry , crystallography , single bond , cleavage (geology) , substrate (aquarium) , enzyme , computational chemistry , inorganic chemistry , catalysis , organic chemistry , physics , alkyl , geotechnical engineering , oceanography , fracture (geology) , geology , engineering , condensed matter physics
We have performed a computational study of substrate CH bond activation in enzymes of the XO family. The CH H‐atom for all XO substrates studied is transferred to the terminal sulfido at the transition state with near neutral charge, and this is consistent with both MoS π → CH σ * and CH σ →MoS π * donoracceptor interactions activating the CH bond. A CH bond scission and Mo reduction appear to be highly correlated along the reaction coordinate for all XO substrates studied, with Mo reduction being a continuous and exponential function of CH bond breaking along the reaction coordinate.