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 plants, the calcium in mollusc shells, or the iron in the hemoglobin in vertebrate animals' red blood cells. The concept of an "element" as an undivisible substance has developed through three major historical phases: Classical definitions (such as those of the ancient Greeks), chemical definitions, and atomic definitions. Ancient philosophy posited a set of classical elements to explain observed patterns in nature. These "elements" originally referred to "earth", "water", "air" and "fire" rather than the chemical elements of modern science. The term 'elements' ("stoicheia") was first used by the Greek philosopher Plato in about 360 BCE in his dialogue Timaeus,