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In biochemistry, denaturation is a process in which proteins or nucleic acids lose folded structure present in their native state due to various factors, including application of some external stress or compound, such as a strong acid or base, a concentrated inorganic salt, an organic solvent (e.g., alcohol or chloroform), agitation and radiation, or heat. [3]
In plants, PPO is a plastidic enzyme with unclear synthesis and function. In functional chloroplasts, it may be involved in oxygen chemistry like mediation of pseudocyclic photophosphorylation. [15] Enzyme nomenclature differentiates between monophenol oxidase enzymes (tyrosinases) and o-diphenol:oxygen oxidoreductase enzymes (catechol oxidases).
Enzymes are not rigid, static structures; instead they have complex internal dynamic motions – that is, movements of parts of the enzyme's structure such as individual amino acid residues, groups of residues forming a protein loop or unit of secondary structure, or even an entire protein domain.
Absorbed amino acids are typically used to create functional proteins, but may also be used to create energy. [3] They can also be converted into glucose. [4] This glucose can then be converted to triglycerides and stored in fat cells. [5] Proteins can be broken down by enzymes known as peptidases or can break down as a result of denaturation ...
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:
Oxidoreductases, enzymes that catalyze oxidation-reduction reactions, constitute Class EC 1 of the IUBMB classification of enzyme-catalyzed reactions. [2] Any of these may be called dehydrogenases, especially those in which NAD + is the electron acceptor (oxidant), but reductase is also used when the physiological emphasis on reduction of the substrate, and oxidase is used only when O 2 is the ...
The most widely observed cofactor involved in dioxygenation reactions is iron, but the catalytic scheme employed by these iron-containing enzymes is highly diverse. Iron-containing dioxygenases can be subdivided into three classes on the basis of how iron is incorporated into the active site: those employing a mononuclear iron center, those containing a Rieske [2Fe-2S] cluster, and those ...
It is an enzyme that accepts electrons from electron-transferring flavoprotein in the mitochondrial matrix, and uses these electrons to reduce ubiquinone. [30] This enzyme contains a flavin and a [4Fe–4S] cluster, but, unlike the other respiratory complexes, it attaches to the surface of the membrane and does not cross the lipid bilayer. [31]