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Vanadium bromoperoxidases have been found in bacteria, fungi, marine macro algae (), and marine microalgae which produce brominated organic compounds. [2]It has not been definitively identified as the bromoperoxidase of higher eukaryotes, such as murex snails, which have a very stable and specific bromoperoxidase, but perhaps not a vanadium dependent one. [3]
The enzyme vanadium bromoperoxidase, one of a larger family of bromoperoxidases, catalyzes this reaction in the marine environment. [9] The oceans are estimated to release 1–2 million tons of bromoform and 56,000 tons of bromomethane annually. [ 10 ]
Bromoform was discovered in 1832 by Löwig who distilled a mixture of bromal and potassium hydroxide, as analogous to preparation of chloroform from chloral. [5]Bromoform can be prepared by the haloform reaction using acetone and sodium hypobromite, by the electrolysis of potassium bromide in ethanol, or by treating chloroform with aluminium bromide.
The enzyme is very specific to bromide and physically stable, but has not been characterized as to its active site metal. As of 2019, no specific gene has been assigned to such an enzyme in the snail genome. [5] Such an activity is probably provided by symbiotic Bacillus bacteria instead. [6]
Upon further spectroscopic characterization and investigation of the substrate pool of this enzyme, Dr. Ziegler discovered that this enzyme solely bound FAD molecule that could form a C4a-hydroxyperoxyflavin intermediate, and that this enzyme could oxidize a wide variety of substrates with no common structural features, including phosphines ...
Calvin cycle step 1 (black circles represent carbon atoms) Calvin cycle steps 2 and 3 combined. The enzyme RuBisCO catalyses the carboxylation of ribulose-1,5-bisphosphate, RuBP, a 5-carbon compound, by carbon dioxide (a total of 6 carbons) in a two-step reaction. [6] The product of the first step is enediol-enzyme complex that can capture CO 2 ...
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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]