The newly proposed mechanistic possibilities in reactions catalyzed by hemoproteins are shown.

<p>At the left are two-electron (top) and one-electron (bottom) oxidized enzyme intermediates, giving rise to two-electron (top) and one-electron (lower) oxidized product or intermediates in the center. The final products that could be formed are shown to the right.</p

CYP2E1 kinetics, probed in detail using experimental data and theoretical simulation.

<p>Experimental details are given in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0010601#s4" target="_blank">methods</a> section.</p

Reconstituted CYP2C9 system shows depletion of specific hydroxylated product over time.

<p>Initial concentrations are ∼0.08 uM of CYP2C9  =  CPR, 0.04 to 0.8 uM Cyt<i>b</i>₅, 1 mM NADPH. Other details are mentioned in the experimental section.</p

Analyses of CYP catalyzed peroxidations by Belanger fits.

<p>Kinetic constants shown in the first three columns are average of duplicate experiments (with standard deviation) and 95% confidence intervals respectively.</p

CYP2C9 baculosomes show lowering of specific hydroxylation of diclofenac upon increasing substrate concentration.

<p>A final concentration of 1 mM NADPH was used. 5 and 10 µl of the commercial enzyme preparation was added to 1 ml of the reaction mixture.</p

Kinetics of CPO catalyzed peroxidation of TMPD obtained by varying the peroxide concentration, at constant peroxidative substrate (TMPD).

<p>Initial conditions- pH 3.5, 100 mM phosphate buffer, 30°C, [CPO] = 20 nM.</p

State kinetics of reconstituted CYP2E1 enzymatic system mediated conversion of pNP, checked for reproducibility and precision.

<p>Experimental details are given in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0010601#s4" target="_blank">methods</a> section.</p

The new biphasic fit is plotted for CYP2E1 mediated hydroxylation profile for conversion of pNP from <b>Figure 8</b>.

<p>The new biphasic fit is plotted for CYP2E1 mediated hydroxylation profile for conversion of pNP from <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0010601#pone-0010601-g008" target="_blank"><b>Figure 8</b></a>.</p

The new biphasic fit is plotted for CPO mediated peroxidation profile for conversion of pyrogallol from <b>Figure 4</b><b>.</b>

<p>The new biphasic fit is plotted for CPO mediated peroxidation profile for conversion of pyrogallol from <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0010601#pone-0010601-g004" target="_blank"><b>Figure 4</b></a><b>.</b></p

Analyses of CPO catalyzed peroxidations by Belanger fits.

<p>Kinetic constants shown in the first three columns are average of duplicate experiments (with standard deviation) and 95% confidence intervals respectively.</p><p>*pH 3, CPO = 1.8 nM, 25°C.</p