Abstract:By treating the reduced MoFe protein from Azotobacter vinelandii with o-phenanthroIi e and O2, partially deficient in both FeMoco and P-cluster and inactive protein could be o rained. After incubating the treated protein with a reconstituent solution containing K2CrO4, ferric homocitrate, Na2S and dithiothreitol, a reactivated protein could be obtained. The absorption spectrum, circular dichroism spectrum, and the C2H2 and proton reduction activities of the reactivated protein were remarkably recovered. However, the spectra were somewhat different from those of the reduced MoFe protein. The results showed that some of the reactivated protein might be Cr-containing protein (CrFe protein) which were similar in function, but somewhat different in structure from MoFe protein.