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In reactions involving donation of a hydrogen atom, oxygen is reduced to water (H 2 O) or hydrogen peroxide (H 2 O 2). Some oxidation reactions, such as those involving monoamine oxidase or xanthine oxidase, typically do not involve free molecular oxygen. [1] [2] The oxidases are a subclass of the oxidoreductases. The use of dioxygen is the ...
For example, an enzyme that catalyzed this reaction would be an oxidoreductase: A – + B → A + B – In this example, A is the reductant (electron donor) and B is the oxidant (electron acceptor). In biochemical reactions, the redox reactions are sometimes more difficult to see, such as this reaction from glycolysis:
Free radical reactions are redox reactions that occur as part of homeostasis and killing microorganisms. In these reactions, an electron detaches from a molecule and then re-attaches almost instantly. Free radicals are part of redox molecules and can become harmful to the human body if they do not reattach to the redox molecule or an antioxidant.
Examples of substances that are common reducing agents include hydrogen, Carbon monoxide, the alkali metals, formic acid, [1] oxalic acid, [2] and sulfite compounds. In their pre-reaction states, reducers have extra electrons (that is, they are by themselves reduced) and oxidizers lack electrons (that is, they are by themselves oxidized).
The redox reactions of nicotinamide adenine dinucleotide. The compound accepts or donates the equivalent of H −. [6] Such reactions (summarized in formula below) involve the removal of two hydrogen atoms from the reactant (R), in the form of a hydride ion (H −), and a proton (H +).
Depiction of common redox reactions in the environment. Adapted from figures by Zhang [1] and Gorny. [2] Redox pairs are listed with the oxidizer (electron acceptor) in red and the reducer (electron donator) in black. Relative favorability of redox reactions in marine sediments based on energy.
Four varieties are recognized by the International Union of Biochemistry and Molecular Biology (IUBMB), cytochromes a, cytochromes b, cytochromes c and cytochrome d. [1] Cytochrome function is linked to the reversible redox change from ferrous (Fe(II)) to the ferric (Fe(III)) oxidation state of the iron found in the heme core. [2]
Ferredoxins (from Latin ferrum: iron + redox, often abbreviated "fd") are iron–sulfur proteins that mediate electron transfer in a range of metabolic reactions. The term "ferredoxin" was coined by D.C. Wharton of the DuPont Co. and applied to the "iron protein" first purified in 1962 by Mortenson, Valentine, and Carnahan from the anaerobic bacterium Clostridium pasteurianum.