Cofactors and Chemisry

Heme

Chemical structure Heme (protoporphyrin IX)
There are several variants, but these are not shown
3D representation of Heme
Hemes are involved in many processes. Oxygen transport and electron transfer as well as chemical oxidations especially in steroid synthesis and drug metabolism
Electron Transfer

Representation of electron transfer with hemes like in cytochrome c. The ellipse represents the ring structure, the red circle the central iron atom. Simple Transfer... one in - one out. The iron cycle between the +2 and +3 redox states.

Reversible Oxygen binding

Representation of reversible oxygen binding like in hemoglobin. The ellipse represents the ring structure, the red circle the central iron atom. Simple reversible binding of molecular oxygen. Note the heme must stay in the +2 state throughout.

Oxidation of substance with molecular oxygen by P450

Simplified Representation of a P450 catalytic cycle. The ellipse represents the ring structure, the red circle the central iron atom. The six membered ring is not to represent cyclohexane in this case, but rather a nondescript substrate. Many P450 enzymes can act on a wide range of substances. The catalytic cycle is very complex and is still being studied intensively. some of the steps are "poorly" shown here.

Note: the P450 moniker is a throwback to the beginnings of biochemistry. Before we knew anything about how this enzyme worked or what it did, it was noted that this type of protein exhibited a unique spectrum in with visible light that had a peak absorption at 450nm.

SOME ENZYMES (PROTEINS) USING THIS COFACTOR
hemoglobin / myoglobin Protein essential for transportation of Oxygen in the blood from lungs to all other tissues
cytochrome c Essential for electron transfer in the oxidative phosphorylation pathway. we will learn more about this protein in module 7
cytochrome P-450's Class of enzymes essential for many different chemistries; most dependent on molecular oxygen: Drug metabolism, steroid synthesis