The subunit structure of nitrite reductase purified from the denitrifier Achromobacter cycloclastes
1999
Inatomi, K. (Mitsubishi Electric Corp., Amagasaki, Hyogo (Japan))
The copper-containing nitrite reductase of Achromobacter cycloclastes has been considered to be a homotrimer with three identical subunits both in the crystal and in solution. In this study, however, the enzyme was found to be a heterotrimer consisting of two subunits with molecular masses of 37 kDa and 36.2 kDa, and the 37 kDa subunit was 6 amino acid residues longer than the smaller subunit. Signal-peptide cleavage sites in its N-terminal region are discussed
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