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 of an element to exist in one of many structural forms is known as 'allotropy'. The standard state, also known as the reference state, of an element is defined as its thermodynamically most stable state at a pressure of 1 bar and a given temperature (typically at 298.15 K). In thermochemistry, an element is defined to have an enthalpy of formation of zero in its standard state. For example, the reference state for carbon is graphite, because the structure of graphite is more stable than that of the other allotropes. Several kinds of descriptive categorizations can be applied broadly to