Cobalt chelatase Cobalt chelatase Cobalt chelatase () is an enzyme that catalyzes the chemical reaction The 4 substrates of this enzyme are ATP, hydrogenobyrinic acid a,c-diamide, Co, and HO, whereas its 4 products are ADP, phosphate, cob(II)yrinic acid a,c-diamide, and H. The aerobic cobalt chelatase (aerobic cobalamin biosynthesis pathway) consists of three subunits, CobT, CobN () and CobS (). Cobalamin (vitamin B12) can be complexed with metal via the ATP-dependent reactions (aerobic pathway) (e.g., in "Pseudomonas denitrificans") or via ATP-independent reactions (anaerobic pathway) (e.g., in "Salmonella typhimurium"). The corresponding cobalt chelatases are not homologous. However, aerobic cobalt chelatase subunits CobN and CobS
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