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The influence of cytochrome b5 on naphthalene oxidation catalyzed by human cytochrome P450 1A2
Stránský, Jaroslav ; Martínek, Václav (advisor) ; Moserová, Michaela (referee)
Cytochromes P450 (CYP) form a crucial group of oxidoreductase-class enzymes participating in the biotransformation of numerous endo- and exogenous compounds (xenobiotics). A negative aspect to the activity of this enzyme, however, can be the bioactivation, a process during which an originally only slightly toxic compound is transformed into a substance of much higher toxicity. Cytochrome P450 has therefore long been standing at the forefront of biochemical and medicinal interest. For the proper function of cytochrome P450 a supply of electrons into a catalytic cycle is necessary. This is usually taken care of by NADPH:cytochrome P450 oxidoreductase. Cytochrome b5, an enzyme present in the membrane of the endoplasmic reticulum of eukaryotic cells along with NADPH:cytochrome P450 oxidoreductase and cytochrome P450, however, can also act as an alternative electron donor. The participation of cytochrome b5 in the catalytic cycle of cytochrome P450 have a potential to modulate this cycle. Over the course of evolution, many isoforms of cytochrome P450 have developed, each possessing different substrate specifity, catalytic properties, distributions within various tissues etc. This bachelor thesis is focused on the isoform 1A2 (CYP1A2) which represents nearly 10 % of all human hepatic cytochrome P450s....
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