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 stable cobalt isotope and the only isotope that exists naturally on Earth. Twenty-two radioisotopes have been characterized; the most stable, Co has a half-life of 5.2714 years, and Co has a half-life of 271.8 days, Co a half-life of 77.27 days, and Co a half-life of 70.86 days. All the other radioactive isotopes of cobalt have half-lives shorter than 18 hours, and in most cases shorter than 1 second. This element also has 4 meta states, all of which have half-lives shorter than 15 minutes. The isotopes of cobalt range in atomic weight from 50 u (Co) to 73 u