Evidence for distinct rate-limiting steps in the cleavage of alkenes by carotenoid cleavage dioxygenases.

ABSTRACT: Carotenoid cleavage dioxygenases (CCDs) use a nonheme Fe(II) cofactor to split alkene bonds of carotenoid and stilbenoid substrates. The iron centers of CCDs are typically five-coordinate in their resting states, with solvent occupying an exchangeable site. The involvement of this iron-bound solvent in CCD catalysis has not been experimentally addressed, but computational studies suggest two possible roles. 1) Solvent dissociation provides a coordination site for O₂, or 2) solvent remains bound to iron but changes its equilibrium position to allow O₂ binding and potentially acts as a proton source. To test these predictions, we investigated isotope effects (H₂O versus D₂O) on two stilbenoid-cleaving CCDs, Novosphingobium aromaticivorans

SUBMITTER: Khadka N 

PROVIDER: S-EPMC6615678 | biostudies-literature | 2019 Jul

REPOSITORIES: biostudies-literature