Methoxatin (Pqq), Coenzyme for Copper-Dependent Amine and Mixed-Function Oxidation in Mammalian Tissues
- 1 January 1989
- journal article
- review article
- Published by Taylor & Francis in Connective Tissue Research
- Vol. 20 (1-4) , 251-257
- https://doi.org/10.3109/03008208909023895
Abstract
The newly discovered coenzyme PQQ can now be measured at picomole levels with redox cycling methods developed in our laboratory. PQQ-peptides have been obtained from digests of the copper quinoenzymes, diamine oxidase, lysyl oxidase and dopamine-β-hydroxylase. PQQ is present in egg yolk and milk, suggesting its immediate availability for developing embryos and newborn animals. We suggest that PQQ, when exposed in traumatized, ischemic, inflammed or pathological tissues, may catalyze the formation of large amounts of superoxide and should be considered as a source of oxidative stress when planning pharmacotherapeutic intervention. PQQ and quinoproteins play a role in the redox metabolism and structural integrity of cells and tissues.Keywords
This publication has 6 references indexed in Scilit:
- The amplefied detection of free and bound methoxatin (PQQ) with nitroblue tetrazolium redox reactions: Insights into the PQQ-locusBiochemical and Biophysical Research Communications, 1988
- Cofactors in and as posttranslational protein modificationsThe FASEB Journal, 1988
- Mammalian Choline Dehydrogenase Is a QuinoproteinAgricultural and Biological Chemistry, 1985
- Total synthesis of the quinonoid alcohol dehydrogenase coenzyme (1) of methylotrophic bacteriaJournal of the American Chemical Society, 1981
- The prosthetic group of methanol dehydrogenase. Purification and some of its propertiesBiochemical Journal, 1980
- A novel coenzyme from bacterial primary alcohol dehydrogenasesNature, 1979