Title : Myeloperoxidase oxidation states involved in myeloperoxidase-oxidase oxidation of thiols.

Pub. Date : 1988 Dec 15

PMID : 2852003






9 Functional Relationships(s)
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Protein Name
Organism
1 Myeloperoxidase oxidation states involved in myeloperoxidase-oxidase oxidation of thiols. Sulfhydryl Compounds myeloperoxidase Homo sapiens
2 Myeloperoxidase oxidation states involved in myeloperoxidase-oxidase oxidation of thiols. Sulfhydryl Compounds myeloperoxidase Homo sapiens
3 The changes in the oxidation state of the leucocyte enzyme myeloperoxidase, induced by buffer and thiols, were studied with visible-light-absorption spectroscopy. Sulfhydryl Compounds myeloperoxidase Homo sapiens
4 These minute amounts of reduced oxygen species are suggested to account for the initiation of myeloperoxidase-oxidase oxidation of thiols. Sulfhydryl Compounds myeloperoxidase Homo sapiens
5 Myeloperoxidase was found to be in its Compound III oxidation state during myeloperoxidase-oxidase oxidation of thiols. Sulfhydryl Compounds myeloperoxidase Homo sapiens
6 Myeloperoxidase was found to be in its Compound III oxidation state during myeloperoxidase-oxidase oxidation of thiols. Sulfhydryl Compounds myeloperoxidase Homo sapiens
7 However, myeloperoxidase-mediated oxidation of thiols with concomitant O2 consumption can also occur with myeloperoxidase in its Compound II oxidation state. Sulfhydryl Compounds myeloperoxidase Homo sapiens
8 However, myeloperoxidase-mediated oxidation of thiols with concomitant O2 consumption can also occur with myeloperoxidase in its Compound II oxidation state. Sulfhydryl Compounds myeloperoxidase Homo sapiens
9 These studies indicate that the ferro and Compound III oxidation states may not be essential intermediates in myeloperoxidase-oxidase oxidation of thiols, but rather that the formation of the Compound III oxidation state retards the reaction. Sulfhydryl Compounds myeloperoxidase Homo sapiens