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 named mendelevium in honor of D.I. Mendeleev, the first to arrange the elements in a periodic manner. Most recently, the synthesis of element 118 (since named oganesson) was reported in October 2006, and the synthesis of element 117 (tennessine) was reported in April 2010. Ten materials familiar to various prehistoric cultures are now known to be chemical elements: Carbon, copper, gold, iron, lead, mercury, silver, sulfur, tin, and zinc. Three additional materials now accepted as elements, arsenic, antimony, and bismuth, were recognized as distinct substances prior to 1500 AD. Phosphorus, cobalt, and platinum were isolated before 1750. Most of the