Achromobacter cycloclastes nitrite reductase. The function of copper, amino acid composition, and ESR spectra.
1. Dialysis against cyanide at pH 7 of Achromobacter cycloclastes nitrite reductase [EC 1.7.99.3] of a dissimilatory type led to the removal of about 50% of the copper from the enzyme molecule, with a concomitant decrease of the enzymatic activities. It was inferred that enzyme-bound copper atoms play an essential role in the catalytic activities of the enzyme. 2. The amino acid composition of the enzyme was determined after acid hydrolysis. 3. ESR spectra of the frozen solution and lyophilized powder of the nitrite reductase predominantly showed the presence of two kinds of copper: Type 1 Cu2+, which had narrow and sharp hyperfine splitting, and Type 2 Cu2+, which had broader hyperfine splitting. The bond between the oxidized enzyme and nitrite seems to be ionic.
D000421:Alcaligenes / Q000201:enzymology*; D000596:Amino Acids / Q000032:analysis*; D001665:Binding Sites; D003300:Copper / Q000502:physiology; D003460:Crystallization; D003486:Cyanides / Q000494:pharmacology; D004578:Electron Spin Resonance Spectroscopy; D009247:NADH, NADPH Oxidoreductases / Q000378:metabolism; D009572:Nitrite Reductases / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation
D000596:Amino Acids; D003486:Cyanides; D003300:Copper; D009247:NADH, NADPH Oxidoreductases; D009572:Nitrite Reductases