Sandbox 177: Difference between revisions
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''In vivo'' CYPOR is believe to alternate between a one and a three electron reduced form. While the 1 electron form is fairly stable, forming a neutral blue semiquinone, it is the hydroquinone, or 3 electron form, that is able to donate electrons to the desired redox partners. | ''In vivo'' CYPOR is believe to alternate between a one and a three electron reduced form. While the 1 electron form is fairly stable, forming a neutral blue semiquinone, it is the hydroquinone, or 3 electron form, that is able to donate electrons to the desired redox partners. | ||
As part of the microsomal electron transport system, CYPOR moves electrons from NADPH -> FAD -> FMN -> cytochrome P450. Specifically a hydride anion is moved from NADPH to the FAD. The two electrons are then individually passed to FMN, in a process that is believed to be conformationally gated, before being passed on to cytochrome P450, again one at a time.<ref name="5TSON"/> This reduction of cytochrome P450 allows it to function in biosynthesis and biodegradation pathways of a variety of endogenous and foreign hydrophobic substrates, including drugs and steroids (2,6).<ref name="5TSON"/> | As part of the microsomal electron transport system, CYPOR moves electrons from NADPH -> FAD -> FMN -> cytochrome P450. Specifically a hydride anion is moved from NADPH to the FAD. The two electrons are then individually passed to FMN, in a process that is believed to be conformationally gated, before being passed on to cytochrome P450, again one at a time.<ref name="5TSON"/> This reduction of cytochrome P450 allows it to function in biosynthesis and biodegradation pathways of a variety of endogenous and foreign hydrophobic substrates, including drugs and steroids (2,6).<ref name="5TSON"/><ref name="2TSON">PMID:7743131</ref> | ||
Cytochrome b5, cytochrome c and heme oxygenase can also receive electrons from CYPOR.<ref name="5TSON"/> In these cases CYPOR is functioning in the heme degradation pathway, or with monooxygenase and/or 7-dehydrocholesterol reductase in sterol synthesis.<ref name="5TSON"/> | Cytochrome b5, cytochrome c and heme oxygenase can also receive electrons from CYPOR.<ref name="5TSON"/> In these cases CYPOR is functioning in the heme degradation pathway, or with monooxygenase and/or 7-dehydrocholesterol reductase in sterol synthesis.<ref name="5TSON"/> | ||
A function that is of particular interest currently is CYPOR’s ability to activate anticancer prodrugs reductively.<ref name="5TSON"/> This makes it a potential target for anticancer research and therapy.<ref name="5TSON"/> | A function that is of particular interest currently is CYPOR’s ability to activate anticancer prodrugs reductively.<ref name="5TSON"/> This makes it a potential target for anticancer research and therapy.<ref name="5TSON"/> | ||
==References== | |||
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