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.
Methane monooxygenase (MMO) is an enzyme capable of oxidizing the C-H bond in methane as well as other alkanes. Methane monooxygenase belongs to the class of oxidoreductase enzymes.
In enzymology, an anthranilate 1,2-dioxygenase (deaminating, decarboxylating) (EC 1.14.12.1) is an enzyme that catalyzes the chemical reaction
In enzymology, an anthranilate 3-monooxygenase (deaminating) (EC 1.14.13.35) is an enzyme that catalyzes the chemical reaction
In enzymology, a benzoate 1,2-dioxygenase (EC 1.14.12.10) is an enzyme that catalyzes the chemical reaction
In enzymology, a benzoate 4-monooxygenase (EC 1.14.14.92, Formerly EC 1.14.13.12) is an enzyme that catalyzes the chemical reaction
In enzymology, a camphor 1,2-monooxygenase (EC 1.14.15.2) is an enzyme that catalyzes the chemical reaction
In enzymology, a camphor 5-monooxygenase (EC 1.14.15.1) is an enzyme that catalyzes the chemical reaction
In enzymology, a cholestanetriol 26-monooxygenase (EC 1.14.13.15) is an enzyme that catalyzes the chemical reaction
In enzymology, a CMP-N-acetylneuraminate monooxygenase (EC 1.14.18.2) is an enzyme that catalyzes the chemical reaction
Ecdysone 20-monooxygenase (EC 1.14.99.22) is an enzyme that catalyzes the chemical reaction
Alkylglycerol monooxygenase (AGMO) is an enzyme that catalyzes the hydroxylation of alkylglycerols, a specific subclass of ether lipids. This enzyme was first described in 1964 as a pteridine-dependent ether lipid cleaving enzyme. In 2010 finally, the gene coding for alkylglycerol monooxygenase was discovered as transmembrane protein 195 (TMEM195) on chromosome 7. In analogy to the enzymes phenylalanine hydroxylase, tyrosine hydroxylase, tryptophan hydroxylase and nitric oxide synthase, alkylglycerol monooxygenase critically depends on the cofactor tetrahydrobiopterin and iron.
In enzymology, a hydroxyphenylacetonitrile 2-monooxygenase (EC 1.14.13.42) is an enzyme that catalyzes the chemical reaction
In enzymology, a lithocholate 6beta-hydroxylase (EC 1.14.13.94) is an enzyme that catalyzes the chemical reaction
In enzymology, a pyrimidine-deoxynucleoside 2'-dioxygenase (EC 1.14.11.3) is an enzyme that catalyzes the chemical reaction
In enzymology, a steroid 11beta-monooxygenase (EC 1.14.15.4) is an enzyme that catalyzes the chemical reaction
In enzymology, a trans-cinnamate 4-monooxygenase (EC 1.14.14.91) is an enzyme that catalyzes the chemical reaction
In enzymology, an unspecific monooxygenase (EC 1.14.14.1) is an enzyme that catalyzes the chemical reaction
In enzymology, a rubredoxin-NAD+ reductase (EC 1.18.1.1) 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.
