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 isotopes: specifically the elements without any stable isotopes are technetium (atomic number 43), promethium (atomic number 61), and all observed elements with atomic numbers greater than 82. Of the 80 elements with at least one stable isotope, 26 have only one single stable isotope. The mean number of stable isotopes for the 80 stable elements is 3.1 stable isotopes per element. The largest number of stable isotopes that occur for a single element is 10 (for tin, element 50). The mass number of an element, "A", is the number of nucleons (protons and neutrons) in the atomic nucleus. Different isotopes