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-59 nuclear magnetic resonance Cobalt-59 nuclear magnetic resonance Cobalt-59 nuclear magnetic resonance is a form of nuclear magnetic resonance spectroscopy that uses cobalt-59, a cobalt isotope. Co is a nucleus of spin 7/2 and 100% abundancy. The nucleus has a magnetic quadrupole moment. Among all NMR active nuclei, Co has the largest chemical shift range and the chemical shift can be correlated with the spectrochemical series. Resonances are observed over a range of 20000 ppm, the width of the signals being up to 20 kHz. A widely used standard is potassium hexacyanocobaltate (0.1M KCo(CN) in DO), which, due to its high symmetry, has a