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 boride Cobalt boride nanoparticless in the size range of 18 to 22 nm have also been produced. When used as a catalyst, cobalt boride is prepared by reducing a cobalt salt, such as Cobalt(II) nitrate, with sodium borohydride. Prior to reduction, the surface area of the catalyst is maximized by supporting the salt on another material; often this material is activated carbon. Cobalt boride Cobalt borides are inorganic compounds with the general formula CoB. The two main cobalt borides CoB and CoB. These are refractory materials. Cobalt boride is known to be exceptionally resistant to oxidation, a chemical property which makes