Radiation inactivation of assimilatory NADH:nitrate reductase from Chlorella. Catalytic and physical sizes of functional units.
作者： L P Solomonson , M J McCreery
DOI: 10.1016/S0021-9258(17)36167-7
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摘要: Assimilatory NADH:nitrate reductase from Chlorella is a homotetramer which contains one of each the prosthetic groups FAD, heme, and Mo6+ per 100-kDa subunit. At low protein concentrations, this tetramer dissociates to fully active dimer. To further elucidate possible relationship between quaternary structure activity, functional size nitrate was determined by radiation inactivation analysis at high concentrations enzyme where principal physical species would be either tetrameric or dimeric, respectively. In both cases, obtained method 100 kDa, suggesting that subunit in dimer can function independently. These results confirm earlier indicated subunits are identical full complement groups. We also found sizes partial activities NADH:cytochrome c reductase, NADH:ferricyanide reduced methyl viologen:nitrate were fractions (approximately 58 47 28 respectively) molecular mass, these domains functionally independent.
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