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
Chemical element so long (at least 100 million times longer than the estimated age of the universe) that their radioactive decay has yet to be detected by experiment. Elements with atomic numbers 83 through 94 are unstable to the point that their radioactive decay can be detected. Three of these elements, bismuth (element 83), thorium (element 90), and uranium (element 92) have one or more isotopes with half-lives long enough to survive as remnants of the explosive stellar nucleosynthesis that produced the heavy elements before the formation of our solar system. For example, at over 1.9 years, over a billion times longer