The mechanism-based inactivation of 2,3-dihydroxybiphenyl 1,2-dioxygenase by catecholic substrates.

  title={The mechanism-based inactivation of 2,3-dihydroxybiphenyl 1,2-dioxygenase by catecholic substrates.},
  author={Fr{\'e}d{\'e}ric H. Vaillancourt and Genevi{\`e}ve Labb{\'e} and Nathalie M. Drouin and Pascal D Fortin and Lindsay D Eltis},
  journal={The Journal of biological chemistry},
  volume={277 3},
2,3-Dihydroxybiphenyl 1,2-dioxygenase (EC ), the extradiol dioxygenase of the biphenyl biodegradation pathway, is subject to inactivation during the steady-state cleavage of catechols. Detailed analysis revealed that this inactivation was similar to the O(2)-dependent inactivation of the enzyme in the absence of catecholic substrate, resulting in oxidation of the active site Fe(II) to Fe(III). Interestingly, the catecholic substrate not only increased the reactivity of the enzyme with O(2) to… CONTINUE READING


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