Unraveling the catalytic mechanism of lactoperoxidase and myeloperoxidase.
Although belonging to the widely investigated peroxidase superfamily, lactoperoxidase (LPO) and myeloperoxidase (MPO) share structural and functional features that make them peculiar with respect to other enzymes of the same group. A survey of the available literature on their catalytic intermediates enabled us to ask some questions that remained unanswered. These questions concern controversial features of the LPO and MPO catalytic cycle, such as the existence of Compound I and Compound II isomers and the identification of their spectroscopic properties. After addressing each of these questions, we formulated a hypothesis that describes an integrated vision of the catalytic mechanism of both enzymes. The main points are: (a) a re-evaluation of the role of superoxide as a reductant in the catalytic cycle; (b) the existence of Cpd I isomers; (c) reciprocal interactions between catalytic intermediates and (d) a mechanistic explanation for catalase activity in both enzymes.
Ghibaudi
Elena
E
Dipartimento di Chimica I.F.M., Università di Torino, Italy. elena.gibaudi@unito.it
Laurenti
Enzo
E
D002384:Catalysis; D004789:Enzyme Activation; D007784:Lactoperoxidase / Q000737:chemistry* / Q000378:metabolism*; D009195:Peroxidase / Q000737:chemistry* / Q000378:metabolism*; D013056:Spectrophotometry, Ultraviolet; D013379:Substrate Specificity
D007784:Lactoperoxidase; D009195:Peroxidase