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 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 and sodium hydroxide, followed by oxidation with ozone. The green form, formerly thought to be cobalt(II) peroxide, apparently requires carbon dioxide as a catalyst. It can be prepared by adding hydrogen peroxide to a solution of cobalt(II) chloride in 96% ethanol