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
Isotopes of cobalt an excited state of the Fe nucleus, which in turn decays to the ground state with emission of a gamma ray. Measurement of the gamma ray spectrum provides information about the chemical state of the iron atom in the sample. Isotopes of cobalt Naturally occurring cobalt (Co) is composed of 1 stable isotope, Co. 28 radioisotopes have been characterized with the most stable being Co with a half-life of 5.2714 years, Co with a half-life of 271.8 days, Co with a half-life of 77.27 days, and Co with a half-life of 70.86 days. All of the remaining radioactive isotopes have