Look over the diagram
See where it says CO?
See where it says FeV?
If you had truly dug to find the meaning of COVFEFE
Don't you think you may have stumbled across this?
https://en.m.wikipedia.org/wiki/Cytochrome_P450
The active site of cytochrome P450contains a heme-iron center. The iron is tethered to the protein via a cysteine thiolate ligand. This cysteine and several flanking residues are highly conserved in known CYPs, and have the formal PROSITE signature consensus pattern [FW] - [SGNH] - x - [GD] - {F} - [RKHPT] - {P} - C - [LIVMFAP] - [GAD].[12] Because of thevast variety of reactions catalyzed by CYPs, the activities and properties of the many CYPs differ in many aspects.[13] In general, the P450 catalytic cycle proceeds as follows:
I highlighted the important parts.
Heme, because Malaria impairs heme metabolism and malaria medicines fix this. In other words, malaria medicine is not a bullet against the microorganism, instead it stops disruption of heme biochemistry
As with other quinoline antimalarial drugs, the antimalarial mechanism of action of quinine has not been fully resolved. The most accepted model is based on hydrochloroquinine and involves the inhibition of hemozoin biocrystallization, which facilitates the aggregation of cytotoxic heme. Free cytotoxic heme accumulates in the parasites, causing death
Cytochrome P450-mediated metabolism of vitamin D
https://www.jlr.org/article/S0022-2275(20)31738-7/fulltext
And lets not forget that exposure to sunlight allows the body to convert LDL cholesterol into Vitamin D. That's why the Cabal calls it BAD Cholesterol because you don't get sick and pay your life savings into their Big Pharma products
The vitamin D signal transduction system involves a series of cytochrome P450-containing sterol hydroxylases to generate and degrade the active hormone, 1α,25-dihydroxyvitamin D3, which serves as a ligand for the vitamin D receptor-mediated transcriptional gene expression described in companion articles in this review series. This review updates our current knowledge of the specific anabolic cytochrome P450s involved in 25- and 1α-hydroxylation, as well as the catabolic cytochrome P450 involved in 24- and 23-hydroxylation steps, which are believed to initiate inactivation of the vitamin D molecule. We focus on the biochemical properties of these enzymes; key residues in their active sites derived from crystal structures and mutagenesis studies; the physiological roles of these enzymes as determined by animal knockout studies and human genetic diseases; and the regulation of these different cytochrome P450s by extracellular ions and peptide modulators. We highlight the importance of these cytochrome P450s in the pathogenesis of kidney disease, metabolic bone disease, and hyperproliferative diseases, such as psoriasis and cancer; as well as explore potential future developments in the field.