Reductive dehaholagenses (EC 1.97.1.8) are a group of enzymes utilized in organohalide respiring bacteria. [1] [2] These enzymes are mostly attached to the periplasmic side of the cytoplasmic membrane and play a central role in energy-conserving respiratory process for organohalide respiring bacteria by reducing organohalides. During such reductive dehalogenation reaction, organohalides are used as terminal electron acceptors. They catalyze the following general reactions:
These membrane-associated enzymes have attracted great interest for the detoxification of organohalide pollutants. Organohalide pollution is a serious global environmental issue affecting soil and groundwater; and reductive dehalogenases offer a promising natural tool for bioremediation.
Reductive dehalogenases are related to the cobamide (or vitamin B12) family of enzymes. They contain a cobalamin at its catalytic active site, where actual reductive reaction occurs. They also harbor iron− sulfur clusters that supply the reducing equivalents. [1] [3] All membrane-associated dehalogenases harbor a N-terminal twin-arginine (TAT) signal sequence (RRXFXK), which is a conserved signal peptide for membrane protein translocation. Monomeric as well as dimeric forms were previously reported.
Enzymatic mechanism is still understudied; however, several studies reported various mechanisms involving an organocobalt adduct, a single-electron transfer, and a halogen–cobalt bond. [1]
The examples are those that can dechlorinate chloroform (TmrA), PCE (PceA), TCE (TceA), and VC (VcrA). [2] Purification of such enzymes in native forms are reportedly difficult; however, a few such enzymes were purified to near homogeneity. [10] [11] Ultracentrifugation, membrane solubilization and a series of liquid chromatography are the commonly employed techniques to the isolation and purification. A chloroform reducing dehalogenase is the latest reductive dehalogenase that was successfully produced and purified. [4]
The researchers in the field had turned their interest to heterologous expression of the same enzymes due to difficulties in obtaining these enzymes in the native form. Only have recently a few recombinant reductive dehalogenases been functionally expressed, bringing the dehalogenase research into next levels. [12] [7] [3] [5] Those successful efforts facilitate further investigations on their biochemical and structural properties.
The first membrane-associated respiratory reductive dehalogenase was heterologously expressed in a soluble and active form and purified using Bacillus megaterium . [5]
In recent years, research on reductive dehalogenases have attracted great interest from both academic and industrial researchers for their potential application in bioremediation of organohalide contamination.
In organochlorine chemistry, reductive dechlorination describes any chemical reaction which cleaves the covalent bond between carbon and chlorine via reductants, to release chloride ions. Many modalities have been implemented, depending on the application. Reductive dechlorination is often applied to remediation of chlorinated pesticides or dry cleaning solvents. It is also used occasionally in the synthesis of organic compounds, e.g. as pharmaceuticals.
A hydrogenase is an enzyme that catalyses the reversible oxidation of molecular hydrogen (H2), as shown below:
Cometabolism is defined as the simultaneous degradation of two compounds, in which the degradation of the second compound depends on the presence of the first compound. This is in contrast to simultaneous catabolism, where each substrate is catabolized concomitantly by different enzymes. Cometabolism occurs when an enzyme produced by an organism to catalyze the degradation of its growth-substrate to derive energy and carbon from it is also capable of degrading additional compounds. The fortuitous degradation of these additional compounds does not support the growth of the bacteria, and some of these compounds can even be toxic in certain concentrations to the bacteria.
Halorespiration or dehalorespiration or organohalide respiration is the use of halogenated compounds as terminal electron acceptors in anaerobic respiration. Halorespiration can play a part in microbial biodegradation. The most common substrates are chlorinated aliphatics, chlorinated phenols and chloroform. Dehalorespiring bacteria are highly diverse. This trait is found in some Campylobacterota, Thermodesulfobacteriota, Chloroflexota, low G+C gram positive Clostridia, and ultramicrobacteria.
Dehalococcoides is a genus of bacteria within class Dehalococcoidia that obtain energy via the oxidation of hydrogen and subsequent reductive dehalogenation of halogenated organic compounds in a mode of anaerobic respiration called organohalide respiration. They are well known for their great potential to remediate halogenated ethenes and aromatics. They are the only bacteria known to transform highly chlorinated dioxins, PCBs. In addition, they are the only known bacteria to transform tetrachloroethene to ethene.
Microbial biodegradation is the use of bioremediation and biotransformation methods to harness the naturally occurring ability of microbial xenobiotic metabolism to degrade, transform or accumulate environmental pollutants, including hydrocarbons, polychlorinated biphenyls (PCBs), polyaromatic hydrocarbons (PAHs), heterocyclic compounds, pharmaceutical substances, radionuclides and metals.
In enzymology, a tetrachloroethene reductive dehalogenase is an enzyme that catalyzes the chemical reaction. This is a member of reductive dehalogenase enzyme family.
In enzymology, a haloalkane dehalogenase (EC 3.8.1.5) is an enzyme that catalyzes the chemical reaction
Iodotyrosine deiodinase, also known as iodotyrosine dehalogenase 1, is a type of deiodinase enzyme that scavenges iodide by removing it from iodinated tyrosine residues in the thyroid gland. These iodinated tyrosines are produced during thyroid hormone biosynthesis. The iodide that is scavenged by iodotyrosine deiodinase is necessary to again synthesize the thyroid hormones. After synthesis, the thyroid hormones circulate through the body to regulate metabolic rate, protein expression, and body temperature. Iodotyrosine deiodinase is thus necessary to keep levels of both iodide and thyroid hormones in balance.
A dehalogenase is a type of enzyme that catalyzes the removal of a halogen atom from a substrate.
Dehalobacter is a genus in the phylum Bacillota (Bacteria).
Dehalococcoidia is a class of Chloroflexota, a phylum of Bacteria. It is also known as the DHC group.
[NiFe] hydrogenase is a type of hydrogenase, which is an oxidative enzyme that reversibly converts molecular hydrogen in prokaryotes including Bacteria and Archaea. The catalytic site on the enzyme provides simple hydrogen-metabolizing microorganisms a redox mechanism by which to store and utilize energy via the reaction
Dehalobacter restrictus is a species of bacteria in the phylum Bacillota. It is strictly anaerobic and reductively dechlorinates tetra- and trichloroethene. It does not form spores; it is a small, gram-positive rod with one lateral flagellum. PER-K23 is its type strain.
Desulfitobacterium dehalogenans is a species of bacteria. They are facultative organohalide respiring bacteria capable of reductively dechlorinating chlorophenolic compounds and tetrachloroethene. They are anaerobic, motile, Gram-positive and rod-shaped bacteria capable of utilizing a wide range of electron donors and acceptors. The type strain JW/IU-DCT, DSM 9161, NCBi taxonomy ID 756499.
Desulfitobacterium chlororespirans is a Gram-positive, anaerobic, spore-forming species of bacteria. Its type strain is Co23. It grows by coupling the oxidation of lactate to the reductive dechlorination of 3-chloro-4-hydroxybenzoate.
Desulfitobacterium hafniense is a species of gram positive bacteria, its type strain is DCB-2T..
Dehalogenimonas lykanthroporepellens is an anaerobic, Gram-negative bacteria in the phylum Chloroflexota isolated from a Superfund site in Baton Rouge, Louisiana. It is useful in bioremediation for its ability to reductively dehalogenate chlorinated alkanes.
Perchlorate reductase is an enzyme that catalyzes the chemical reactions:
Sam Hay is a chemist from New Zealand and a Reader in the Department of Chemistry at The University of Manchester. His research in general is based on computational chemistry and theoretical chemistry, specifically on the areas of In silico Enzymology, quantum mechanics roles in biological processes, kinetic modelling of complex reactions and high pressure spectroscopy.
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