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 these numbers are integers), and also resolves some ambiguities in the chemistry-based view due to varying properties of isotopes and allotropes within the same element. Currently, IUPAC defines an element to exist if it has isotopes with a lifetime longer than the 10 seconds it takes the nucleus to form an electronic cloud. By 1914, seventy-two elements were known, all naturally occurring. The remaining naturally occurring elements were discovered or isolated in subsequent decades, and various additional elements have also been produced synthetically, with much of that work pioneered by Glenn T. Seaborg. In 1955, element 101 was discovered and