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 to cause chemical effects), the isotopes of a given element are chemically nearly indistinguishable. All of the elements have some isotopes that are radioactive (radioisotopes), although not all of these radioisotopes occur naturally. The radioisotopes typically decay into other elements upon radiating an alpha or beta particle. If an element has isotopes that are not radioactive, these are termed "stable" isotopes. All of the known stable isotopes occur naturally (see primordial isotope). The many radioisotopes that are not found in nature have been characterized after being artificially made. Certain elements have no stable isotopes and are composed "only" of radioactive