INTRO - A B C D E F G H I J K L M N O P Q R S T U V-Z - INDEX


F

Farr effect:
The profound increase in oxygen absorption via the pulmonary route, which occurs in vivo during intravenous infusion of a dilute solution of hydrogen peroxide. This was discovered by Charles Farr, M.D., Ph.D. while researching the physiologic effects of hydrogen peroxide.

Fenton reaction:
the reduction of hydrogen peroxide (HOOH) by ferrous cation (Fe++) producing hydroxyl radical (HO*) and hydroxide anion (OH-).

flavin:
a tricyclic compound containing an aromatic ring, a heterocyclic ring, and a lactam ring usually connected to a sugar molecule; the redox active center of flavoproteins; the yellow colored nonribose part of riboflavin (vitamin B2). Flavin is a conjugated diimine which is able to reversibly accept one or two hydrogen atoms at a time. Its highly conjugated structure provides stability to its semireduced radicalized form. It is ubiquitous in living things as an essential cofactor to numerous oxidoreductases and oxygenases.

flavin-adenine-dinucleotide (FAD):
an essential cofactor to numerous oxidoreductases composed of a flavin molecule and an adenine molecule covalently linked by a glycoside bridge. FAD is tightly bound to the apoenzyme that it activates. Its reduced form is symbolized by FADH2.

flavoprotein:
any enzyme (usually an oxidoreductase) utilizing flavin as a cofactor (usually FAD or FMN).

ferric cation (Fe+++):
the more fully oxidized and trivalent form of iron. Fe+++ is a medium strength oxidant. It is poorly soluble in water due to its tendency to form precipitates with numerous anions. It can be suspended or solubilized by various chelators or carrier proteins. Ferric compounds are usually red to brown in color. Numerous oxidoreductases utilize Fe+++ in their active centers due to its facile and reversible conversion by one electron reduction to ferrous cation (Fe++).

ferrous cation (Fe++):
the partially oxidized divalent form of iron. It is a weak oxidant and a weak reductant. It is more readily soluble in water and binds less tightly to chelators and carrier proteins than Fe+++. It is yellowish green in color. Numerous oxidoreductases utilize Fe++ in their active centers due to its facile and reversible conversion by one electron oxidation to Fe+++. Examples include: iron-sulfur centers, cytochromes, and peroxidases. Hemoglobin and myoglobin utilize ferrous iron not as a reductant but as a carrier of diatomic oxygen. Fe++ can reduce numerous compounds of oxygen to either generate or to quench oxyradicals depending on circumstances.

folic acid:
a B vitamin essential to numerous metabolic pathways which metabolize methyl and other single carbon groups. Folic acid must be enzymatically reduced by the addition of four hydrogen atoms supplied by NADPH to become active.

free radical (R*):
a limb or ray of a larger molecule considered to have been broken off by physical or chemical action; any compound containing one or more unpaired electrons. These are highly reactive compounds and are usually very short lived and unstable due to the unpaired electron occupying a molecular orbital capable of holding two spin paired electrons. Free radicals which involve oxygen atoms as the carrier of the unpaired electrons usually behave as strong oxidants and readily form electrophilic adducts to susceptible molecules.

INTRO - A B C D E F G H I J K L M N O P Q R S T U V-Z - INDEX