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-60 intensity gamma-ray emitter with a relatively long half-life, 5.27 years, compared to other gamma ray sources of similar intensity. The β-decay energy is low and easily shielded; however, the gamma-ray emission lines have energies around 1.3 MeV, and are highly penetrating. The main uses for are: Cobalt has been discussed as a "salting" element to add to nuclear weapons, to produce a cobalt bomb, an extremely "dirty" weapon which would contaminate large areas with nuclear fallout, rendering them uninhabitable. In one hypothetical design, the tamper of the weapon would be made of . When the bomb exploded, the excess neutrons