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 rather small line width. Systems of low symmetry can yield broadened signals to an extent that renders the signals unobservable in fluid phase NMR, in these cases signals can still be observable in solid state NMR. 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