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.
The branched-chain α-ketoacid dehydrogenase complex is a multi-subunit complex of enzymes that is found on the mitochondrial inner membrane. This enzyme complex catalyzes the oxidative decarboxylation of branched, short-chain alpha-ketoacids. BCKDC is a member of the mitochondrial α-ketoacid dehydrogenase complex family, which also includes pyruvate dehydrogenase and alpha-ketoglutarate dehydrogenase, key enzymes that function in the Krebs cycle.
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.
Rubredoxins are a class of low-molecular-weight iron-containing proteins found in sulfur-metabolizing bacteria and archaea. Sometimes rubredoxins are classified as iron-sulfur proteins; however, in contrast to iron-sulfur proteins, rubredoxins do not contain inorganic sulfide. Like cytochromes, ferredoxins and Rieske proteins, rubredoxins are thought to participate in electron transfer in biological systems. Recent work in bacteria and algae have led to the hypothesis that some rubredoxins may instead have a role in delivering iron to metalloproteins.
In enzymology, a 6-hydroxynicotinate reductase is an enzyme that catalyzes the chemical reaction
In enzymology, a 2-oxobutyrate synthase (EC 1.2.7.2) is an enzyme that catalyzes the chemical reaction
In enzymology, a 2-oxoglutarate synthase (EC 1.2.7.3) is an enzyme that catalyzes the chemical reaction
In enzymology, a 2-oxoisovalerate dehydrogenase (acylating) (EC 1.2.1.25) is an enzyme that catalyzes the chemical reaction
In enzymology, a 3-methyl-2-oxobutanoate dehydrogenase (EC 1.2.4.4) is an enzyme that catalyzes the chemical reaction
In enzymology, a carbon-monoxide dehydrogenase (ferredoxin) (EC 1.2.7.4) is an enzyme that catalyzes the chemical reaction
In enzymology, a glyceraldehyde-3-phosphate dehydrogenase (ferredoxin) (EC 1.2.7.6) is an enzyme that catalyzes the chemical reaction
In enzymology, an indolepyruvate ferredoxin oxidoreductase (EC 1.2.7.8) is an enzyme that catalyzes the chemical reaction
In enzymology, a pyruvate synthase is an enzyme that catalyzes the interconversion of pyruvate and acetyl-CoA. It is also called pyruvate:ferredoxin oxidoreductase (PFOR).
In enzymology, a ferredoxin-NADP+ reductase (EC 1.18.1.2) abbreviated FNR, is an enzyme that catalyzes the chemical reaction
In enzymology, a rubredoxin—NAD(P)+ reductase (EC 1.18.1.4) is an enzyme that catalyzes the chemical reaction
Superoxide reductase is an enzyme that catalyzes the conversion of highly reactive and toxic superoxide (O2−) into less toxic hydrogen peroxide (H2O2):
In enzymology, a [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] is an enzyme that catalyzes the chemical reaction
A transition metal oxo complex is a coordination complex containing an oxo ligand. Formally O2-, an oxo ligand can be bound to one or more metal centers, i.e. it can exist as a terminal or (most commonly) as bridging ligands (Fig. 1). Oxo ligands stabilize high oxidation states of a metal. They are also found in several metalloproteins, for example in molybdenum cofactors and in many iron-containing enzymes. One of the earliest synthetic compounds to incorporate an oxo ligand is potassium ferrate (K2FeO4), which was likely prepared by Georg E. Stahl in 1702.
(3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring))-phosphatase (EC 3.1.3.52, branched-chain oxo-acid dehydrogenase phosphatase, branched-chain 2-keto acid dehydrogenase phosphatase, branched-chain α-keto acid dehydrogenase phosphatase, BCKDH', [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]-phosphatase, [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)]-phosphate phosphohydrolase) is an enzyme with systematic name (3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring))-phosphate phosphohydrolase. This enzyme catalyses the following chemical reaction
In enzymology, an aldehyde ferredoxin oxidoreductase (EC 1.2.7.5) is an enzyme that catalyzes the chemical reaction
