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(II) oxide Cobalt(II) oxide Cobalt(II) oxide or cobalt monoxide is an inorganic compound that appears as olive-green to red crystals, or as a greyish or black powder. It is used extensively in the ceramics industry as an additive to create blue colored glazes and enamels as well as in the chemical industry for producing cobalt(II) salts. CoO crystals adopt the periclase (rock salt) structure with a lattice constant of 4.2615 Å. It is antiferromagnetic below 16 °C. Cobalt(II,III) oxide decomposes to cobalt(II) oxide at 950 °C: Though commercially available, cobalt(II) oxide may be prepared in the laboratory by electrolyzing a solution of