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 than the current estimated age of the universe, bismuth-209 has the longest known alpha decay half-life of any naturally occurring element. The very heaviest 24 elements (those beyond plutonium, element 94) undergo radioactive decay with short half-lives and cannot be produced as daughters of longer-lived elements, and thus they do not occur in nature at all. The properties of the chemical elements are often summarized using the periodic table, which powerfully and elegantly organizes the elements by increasing atomic number into rows ("periods") in which the columns ("groups") share recurring ("periodic") physical and chemical properties. The current standard table contains