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
Cobalt the 20th century with the stellite alloys, containing chromium with varying quantities of tungsten and carbon. Alloys with chromium and tungsten carbides are very hard and wear-resistant. Special cobalt-chromium-molybdenum alloys like Vitallium are used for prosthetic parts (hip and knee replacements). Cobalt alloys are also used for dental prosthetics as a useful substitute for nickel, which may be allergenic. Some high-speed steels also contain cobalt for increased heat and wear resistance. The special alloys of aluminium, nickel, cobalt and iron, known as Alnico, and of samarium and cobalt (samarium-cobalt magnet) are used in permanent magnets. It is also alloyed with