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 glass cobalt oxide together with quartz and potassium carbonate. The result was an intensive blue glass-like substance that was ground and sold to producers of glassware and porcelain. "Smalt", Bruno Mühlethaler and Jean Thissen, "Studies in Conservation", Vol. 14, No. 2 (May, 1969), pp. 47–61, JSTOR Cobalt glass Cobalt glass—known as "smalt" when ground as a pigment—is a deep blue colored glass prepared by including a cobalt compound, typically cobalt oxide or cobalt carbonate, in a glass melt. Cobalt is a very intense glass colorant and very little is required to show a noticeable amount of color. Cobalt blue glass is