The subunit structure of nitrite reductase purified from the denitrifier Achromobacter cycloclastes

• Published in: Bioscience, biotechnology, and biochemistry Vol. 63; no. 11; pp. 2020 - 2022
• Main Author: Inatomi, K. (Mitsubishi Electric Corp., Amagasaki, Hyogo (Japan))
• Format: Journal Article
• Language: English
• Published: Tokyo Japan Society for Bioscience, Biotechnology, and Agrochemistry 01.11.1999; Japan Society for Bioscience Biotechnology and Agrochemistry; Oxford University Press
• Subjects: Achromobacter cycloclastes; Alcaligenes - enzymology; Amino Acid Sequence; BACTERIA; Bacteriology; Biological and medical sciences; Biology of microorganisms of confirmed or potential industrial interest; Biotechnology; COBRE; COPPER; copper enzyme; CUIVRE; DENITRIFICACION; DENITRIFICATION; ENZIMAS; ENZYME; ENZYMES; Fundamental and applied biological sciences. Psychology; Macromolecular Substances; Metabolism. Enzymes; Microbiology; Miscellaneous; Mission oriented research; Molecular Sequence Data; Molecular Weight; NITRITE REDUCTASE; Nitrite Reductases - chemistry; Nitrite Reductases - isolation & purification; NITRITO REDUCTASA; PEPTIDE; PEPTIDES; PEPTIDOS; periplasmic protein; Protein Structure, Quaternary; PURIFICACION; PURIFICATION; Sequence Alignment; Sequence Homology, Amino Acid; signal peptide; Leader peptide; Purification; Enzyme; Achromobacter cycloclastes; Nitrite reductase; N terminal-Sequence; Bacteria; Oxidoreductases; Subunit; Aminoacid sequence; Structural analysis

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...