Cobalt chelatase are homologous to Mg-chelatase subunits BchH and BchI, respectively. CobT, too, has been found to be remotely related to the third subunit of Mg-chelatase, BchD (involved in bacteriochlorophyll synthesis, e.g., in Rhodobacter capsulatus). This enzyme belongs to the family of ligases, specifically those forming nitrogen-D-metal bonds in coordination complexes. The systematic name of this enzyme class is hydrogenobyrinic-acid-a,c-diamide:cobalt cobalt-ligase (ADP-forming). Other names in common use include hydrogenobyrinic acid a,c-diamide cobaltochelatase, CobNST, and CobNCobST. This enzyme participates in porphyrin and chlorophyll metabolism. Cobalt chelatase Cobalt chelatase () is an enzyme that catalyzes the chemical reaction The 4 substrates of this enzyme
Cobalt with water and oxygen to brown cobalt(III) hydroxide (Co(OH)). At temperatures of 600–700 °C, CoO oxidizes to the blue cobalt(II,III) oxide (CoO), which has a spinel structure. Black cobalt(III) oxide (CoO) is also known. Cobalt oxides are antiferromagnetic at low temperature: CoO (Néel temperature 291 K) and CoO (Néel temperature: 40 K), which is analogous to magnetite (FeO), with a mixture of +2 and +3 oxidation states. The principal chalcogenides of cobalt include the black cobalt(II) sulfides, CoS, which adopts a pyrite-like structure, and cobalt(III) sulfide (CoS). Four dihalides of cobalt(II) are known: cobalt(II) fluoride (CoF, pink), cobalt(II) chloride (CoCl,