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 radial tires. In addition they are used as accelerators in polyester resin systems. Cobalt-based catalysts are used in reactions involving carbon monoxide. Cobalt is also a catalyst in the Fischer–Tropsch process for the hydrogenation of carbon monoxide into liquid fuels. Hydroformylation of alkenes often uses cobalt octacarbonyl as a catalyst, although it is often replaced by more efficient iridium- and rhodium-based catalysts, e.g. the Cativa process. The hydrodesulfurization of petroleum uses a catalyst derived from cobalt and molybdenum. This process helps to clean petroleum of sulfur impurities that interfere with the refining of liquid fuels. Before the 19th century, cobalt