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NotificationsNotify me of updates to Mechanistic Insights into Prostanoid Transformations Catalyzed by Cytochrome P450: Prostacyclin and Thromboxane Biosyntheses pp. 239-264
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Mechanistic Insights into Prostanoid Transformations Catalyzed by Cytochrome P450: Prostacyclin and Thromboxane Biosyntheses pp. 239-264 $100.00
Authors:  (Tetsuya K. Yanai, Seiji Mori, Ibaraki University, Bunkyo, Mito, Japan)
Abstract:
Cytochrome P450s (P450) are an important class of proteins found in living
organisms as they play a critical role in the metabolism of many endogenous and
exogenous molecules. Examples of the former include the metabolites Prostacyclin
(PGI2) and thromboxane A2 (TXA2), which are biosynthesized from the substrate
prostaglandin H2 (PGH2) by the P450s, prostalyclin and thromboxane synthases,
respectively. Both metabolites play a key role in renal, cardiovascular, and pulmonary
diseases so greater mechanistic understanding of the processes leading to their formation
is highly desirable. Unlike typical cytochrome P450 reactions such as monooxygenations,
synthases do not require O2 or electron transfer from reductases for catalytic function.
This is an area of active scientific interest in the area although there are several
mechanistic proposals on the isomerization reactions of PGH2, many aspects of the
reaction still remain unclear. Recent research highlights include resonance Raman
spectroscopic analyses that show the resting state of the thromboxane synthase bound
with a substrate analogue contains a low-spin six coordinate heme. In addition, X-ray
crystallographic studies on prostacyclin synthase indicate that the catalytic pocket is
small and hydrophobic in character. Also worth mention are recent quantum mechanical
(QM) studies that indicates homolytic O−O bond cleavage of PGH2, is followed by one
electron transfer from substrate to the heme, is essential for the generation of TXA2 and
PGI2. In this chapter, we review the basic processes involved in heme and prostanoid
chemistry and discuss the most recent studies in the area. 


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Mechanistic Insights into Prostanoid Transformations Catalyzed by Cytochrome P450: Prostacyclin and Thromboxane Biosyntheses pp. 239-264