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(III) hydroxide at –30 to –35°С, then adding a 15% solution of sodium carbonate in water with intense stirring. The resulting dark green powder is fairly stable at liquid nitrogen temperature, but at room temperature it turns dark brown within a few days. Cobalt(III) hydroxide Cobalt(III) hydroxide or cobaltic hydroxide is a chemical compound with formula or . It is an ionic compound, with trivalent cobalt cations and hydroxyl anions . The compound is known in two structurally different forms, "brownish-black" and "green". The brownish-black form is a stable solid and can be prepared by reaction of water solutions of cobalt(II) chloride