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
Lithium cobalt oxide Lithium cobalt oxide Lithium cobalt oxide, sometimes called lithium cobaltate or lithium cobaltite, is a chemical compound with formula . The cobalt atoms are formally in the +3 oxidation state, hence the IUPAC name lithium cobalt(III) oxide. Lithium cobalt oxide is a dark blue or bluish-gray crystalline solid, and is commonly used in the positive electrodes of lithium-ion batteries. The structure of has been studied with numerous techniques including x-ray diffraction, electron microscopy, neutron powder diffraction, and EXAFS. The solid consists of layers of monovalent lithium cations () that lie between extended anionic sheets of cobalt and oxygen atoms, arranged