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 for californium and Es for einsteinium), are always capitalized (see below). In the second half of the twentieth century, physics laboratories became able to produce nuclei of chemical elements with half-lives too short for an appreciable amount of them to exist at any time. These are also named by IUPAC, which generally adopts the name chosen by the discoverer. This practice can lead to the controversial question of which research group actually discovered an element, a question that delayed the naming of elements with atomic number of 104 and higher for a considerable amount of time. (See element naming controversy).