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 (Co). The primary decay mode for isotopes with atomic mass unit values less than that of the most abundant stable isotope, Co, is electron capture and the primary mode of decay in isotopes with atomic mass greater than 59 atomic mass units is beta decay. The primary decay products below Co are element 26 (iron) isotopes; above that the decay products are element 28 (nickel) isotopes. Cobalt compounds have been used for centuries to impart a rich blue color to glass, glazes, and ceramics. Cobalt has been detected in Egyptian sculpture, Persian jewelry from the third millennium BC, in the