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 whole number. For example, the relative atomic mass of chlorine is 35.453 u, which differs greatly from a whole number as it is an average of about 76% chlorine-35 and 24% chlorine-37. Whenever a relative atomic mass value differs by more than 1% from a whole number, it is due to this averaging effect, as significant amounts of more than one isotope are naturally present in a sample of that element. Chemists and nuclear scientists have different definitions of a "pure element". In chemistry, a pure element means a substance whose atoms all (or in practice almost all) have the