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 is the most stable element that can easily be made from alpha particles (being a product of decay of radioactive nickel-56, ultimately made from 14 helium nuclei). Elements heavier than iron are made in energy-absorbing processes in large stars, and their abundance in the universe (and on Earth) generally decreases with their atomic number. The abundance of the chemical elements on Earth varies from air to crust to ocean, and in various types of life. The abundance of elements in Earth's crust differs from that in the Solar system (as seen in the Sun and heavy planets like Jupiter) mainly