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 sulfide investigated as electrocatalysts. [[Category:Cobalt compounds]] [[Category:Sulfides]] Cobalt sulfide Cobalt sulfide is the name for chemical compounds with a formula CoS. Well-characterized species include minerals with the formula CoS, CoS, CoS, and CoS. In general, the sulfides of cobalt are black, semiconducting, insoluble in water, and nonstoichiometric. Cobalt sulfides occur widely as minerals, comprising major sources of all cobalt compounds. Binary cobalt sulfide minerals include the cattierite (CoS) and linnaeite (CoS). CoS (see image in table) is isostructural with iron pyrite, featuring disulfide groups, i.e. CoS. Linnaeite, also rare, adopts the spinel motif. The CoS compound is known as a very