The cytochrome P450 monooxygenases (P450s) are thiolate heme proteins that can, often
under physiological conditions, catalyze many distinct oxidative transformations on a wide …

The extreme limitation of free iron has driven various pathogens to acquire iron from the host
in the form of heme. Specifically, several Gram-negative pathogens secrete a heme binding …

A recently proposed pathway for heme b biosynthesis, common to diverse bacteria, has the
conversion of two of the four propionates on coproheme III to vinyl groups as its final step …

Resonance Raman (RR) spectroscopy is used to help define active site structural responses
of nanodisc-incorporated CYP3A4 to the binding of three substrates: bromocriptine (BC) …

Raman spectroscopy (RS) is a vibrational spectroscopy technique based on the
phenomenon of inelastic light scattering from matter (the Raman effect). It is a versatile tool …

The first step in the enzymatic cycle of mammalian peroxidases, including lactoperoxidase
(LPO), is binding of hydrogen peroxide to the ferric resting state to form a ferric-hydroperoxo …

The allosteric regulator BAY-41-2272 converts the CO adduct of soluble guanylyl cyclase
(CO− sGC) enzyme from a low-to high-output form, with respect to production of cGMP …

Cytochrome P450 4B1 (4B1) functions in both xenobiotic and endobiotic metabolism. An
ester linkage between Glu-310 in 4B1 and the 5-methyl group of heme facilitates preferential …

An important function of steroidogenic cytochromes P450 is the transformation of cholesterol
to produce androgens, estrogens, and the corticosteroids. The activities of cytochrome …

Resonance Raman studies of P450 2B4 are reported for the substrate-free form and when
bound to the substrates, benzphetamine (BZ) or butylated hydroxytoluene (BHT), the latter …