Perchlorate reductase is an enzyme that catalyzes the chemical reactions:
and
Thus, the substrates of this enzyme are a reduced electron acceptor (denoted AH2) and either chlorate or perchlorate, sometimes collectively denoted as (per)chlorate. The products are chlorite, an oxidized electron acceptor (denoted A), and water. It is closely related to the enzyme chlorate reductase, but is distinguished by its ability to reduce both perchlorate and chlorate, whereas chlorate reductase only acts on chlorate. Perchlorate reductase and chlorate reductase are closely related but form genetically distinct clades. [1]
As of February 2023, perchlorate reductase has not been assigned a specific Enzyme Commission number, but along with chlorate reductase (EC 1.97.1.1), it would presumably be a member of the EC 1.97.1.- oxidoreductase subclass. Some databases, including BRENDA, currently combine perchlorate reductase and chlorate reductase listings. [2]
Perchlorate reductase is usually encoded as a combination of four genes, denoted pcrABCD. [3] The active subunits are pcrA and pcrB which form a periplasmic dimer similar to the active complex in nitrate reductase. pcrC is a believed to be a c-type cytochrome that connects the AB complex to the membrane and allows for electron shuttling. The function of pcrD is uncertain, but may encode a molybdenum-containing chaperone protein specific to assembling the pcrABC system. All known functional perchlorate reductase enzymes include genetically similar versions of pcrABCD except for the Campylobacterota Arcobacter strain CAB, which lacks a traditional pcrC and appears to have replaced it with an unrelated Campylobacterota cytochrome. [4]
All characterized organisms that encode perchlorate reductase also have the enzyme chlorite dismutase, which reduces the chlorite produced by perchlorate reductase, and prevents this reactive compound from accumulating to toxic levels. The pcrABCD and chlorite dismutase gene are typically located together in the bacterial genome.
Anaerobic respiration is respiration using electron acceptors other than molecular oxygen (O2). Although oxygen is not the final electron acceptor, the process still uses a respiratory electron transport chain.
Thermus aquaticus is a species of bacteria that can tolerate high temperatures, one of several thermophilic bacteria that belong to the Deinococcota phylum. It is the source of the heat-resistant enzyme Taq DNA polymerase, one of the most important enzymes in molecular biology because of its use in the polymerase chain reaction (PCR) DNA amplification technique.
A perchlorate is a chemical compound containing the perchlorate ion, ClO−4, the conjugate base of perchloric acid. As counterions, there can be metal cations, quaternary ammonium cations or other ions, for example, nitronium cation.
Cytochromes P450 are a superfamily of enzymes containing heme as a cofactor that mostly, but not exclusively, function as monooxygenases. However, they are not omnipresent; for example, they have not been found in Escherichia coli. In mammals, these enzymes oxidize steroids, fatty acids, xenobiotics, and participate in many biosyntheses. By hydroxylation, CYP450 enzymes convert xenobiotics into hydrophilic derivatives, which are more readily excreted.
Organohalide respiration (OHR) (previously named halorespiration or dehalorespiration) is the use of halogenated compounds as terminal electron acceptors in anaerobic respiration. Organohalide respiration can play a part in microbial biodegradation. The most common substrates are chlorinated aliphatics (PCE, TCE, chloroform) and chlorinated phenols. Organohalide-respiring bacteria are highly diverse. This trait is found in some Campylobacterota, Thermodesulfobacteriota, Chloroflexota (green nonsulfur bacteria), low G+C gram positive Clostridia, and ultramicrobacteria.
Pyrococcus furiosus is a heterotrophic, strictly anaerobic, extremophilic, model species of archaea. It is classified as a hyperthermophile because it thrives best under extremely high temperatures, and is notable for having an optimum growth temperature of 100 °C. P. furiosus belongs to the Pyrococcus genus, most commonly found in extreme environmental conditions of hydrothermal vents. It is one of the few prokaryotic organisms that has enzymes containing tungsten, an element rarely found in biological molecules.
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.
In enzymology, a 4-phosphoerythronate dehydogenase (EC 1.1.1.290) is an enzyme that catalyzes the chemical reaction
In enzymology, a sorbose reductase (EC 1.1.1.289) is an enzyme that catalyzes the chemical reaction
In enzymology, a chlorate reductase (EC 1.97.1.1) is an enzyme that catalyzes the chemical reaction
In enzymology, a tetrachloroethene reductive dehalogenase is an enzyme that catalyzes the chemical reaction. This is a member of reductive dehalogenase enzyme family.
The enzyme chorismate lyase catalyzes the first step in ubiquinone biosynthesis, the removal of pyruvate from chorismate, to yield 4-hydroxybenzoate in Escherichia coli and other Gram-negative bacteria. It belongs to the family of lyases, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is chorismate pyruvate-lyase (4-hydroxybenzoate-forming). Other names in common use include CL, CPL, and UbiC.
In enzymology, a 3-oxoadipyl-CoA thiolase is an enzyme that catalyzes the chemical reaction
Dechloromonas agitata strain CKB is a dissimilatory perchlorate reducing bacterium (DRPB) that was isolated from paper mill waste. Strain CKB is a Gram negative, facultative anaerobe belonging to the Betaproteobacteria. The cells of strain CKB are highly motile and possess a single polar flagellum. D. agitata can couple the oxidation of several electron donors such as acetate, propionate, butyrate, lactate, succinate, fumarate, malate or yeast extract to electron acceptors such as oxygen, chlorate, perchlorate, ferrous iron, sulfide, and reduced humic substances like 2,6-anthrahydroquinone disulfonate. Unlike other perchlorate reducers, strain CKB cannot grow by nitrate reduction, which suggests that the pathways of nitrate and perchlorate reduction are distinct and unrelated, contrary to what previous research had shown.
Arcobacter is a genus of Gram-negative, spiral-shaped bacteria in the phylum Campylobacterota. It shows an unusually wide range of habitats, and some species can be human and animal pathogens. Species of the genus Arcobacter are found in both animal and environmental sources, making it unique among the Campylobacterota. This genus currently consists of five species: A. butzleri, A. cryaerophilus, A. skirrowii, A. nitrofigilis, and A. sulfidicus, although several other potential novel species have recently been described from varying environments. Three of these five known species are pathogenic. Members of this genus were first isolated in 1977 from aborted bovine fetuses. They are aerotolerant, Campylobacter-like organisms, previously classified as Campylobacter. The genus Arcobacter, in fact, was created as recently as 1992. Although they are similar to this other genus, Arcobacter species can grow at lower temperatures than Campylobacter, as well as in the air, which Campylobacter cannot.
The fnr gene of Escherichia coli encodes a transcriptional activator (FNR) which is required for the expression of a number of genes involved in anaerobic respiratory pathways. The FNR protein of E. coli is an oxygen – responsive transcriptional regulator required for the switch from aerobic to anaerobic metabolism.
"Type III mutants, originally frdB, were designated fnr because they were defective in fumarate and nitrate reduction and impaired in their ability to produce gas." - Lambden and Guest, 1976 Journal of General Microbiology97, 145-160
Acetoanaerobium sticklandii is an anaerobic, motile, gram-positive bacterium. It was first isolated in 1954 from the black mud of the San Francisco Bay Area by T.C. Stadtman, who also named the species. A. sticklandii is not pathogenic in humans.
Oxidation response is stimulated by a disturbance in the balance between the production of reactive oxygen species and antioxidant responses, known as oxidative stress. Active species of oxygen naturally occur in aerobic cells and have both intracellular and extracellular sources. These species, if not controlled, damage all components of the cell, including proteins, lipids and DNA. Hence cells need to maintain a strong defense against the damage. The following table gives an idea of the antioxidant defense system in bacterial system.
Arsenate-reducing bacteria are bacteria which reduce arsenates. Arsenate-reducing bacteria are ubiquitous in arsenic-contaminated groundwater (aqueous environment). Arsenates are salts or esters of arsenic acid (H3AsO4), consisting of the ion AsO43−. They are moderate oxidizers that can be reduced to arsenites and to arsine. Arsenate can serve as a respiratory electron acceptor for oxidation of organic substrates and H2S or H2. Arsenates occur naturally in minerals such as adamite, alarsite, legrandite, and erythrite, and as hydrated or anhydrous arsenates. Arsenates are similar to phosphates since arsenic (As) and phosphorus (P) occur in group 15 (or VA) of the periodic table. Unlike phosphates, arsenates are not readily lost from minerals due to weathering. They are the predominant form of inorganic arsenic in aqueous aerobic environments. On the other hand, arsenite is more common in anaerobic environments, more mobile, and more toxic than arsenate. Arsenite is 25–60 times more toxic and more mobile than arsenate under most environmental conditions. Arsenate can lead to poisoning, since it can replace inorganic phosphate in the glyceraldehyde-3-phosphate --> 1,3-biphosphoglycerate step of glycolysis, producing 1-arseno-3-phosphoglycerate instead. Although glycolysis continues, 1 ATP molecule is lost. Thus, arsenate is toxic due to its ability to uncouple glycolysis. Arsenate can also inhibit pyruvate conversion into acetyl-CoA, thereby blocking the TCA cycle, resulting in additional loss of ATP.
The chrB-a RNA motif and chrB-b RNA motif refer to a related, conserved RNA structure that was discovered by bioinformatics. The structures of these motifs are similar, and some genomic locations are predicted to exhibit both motifs. The chrB-b motif has an extra pseudoknot that is not consistently found in chrB-a examples. It was proposed that the two motifs could be unified into one common structure, with additional information.