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Updated: Dec 25, 2025

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
Published on: December 16, 2013
Unique hexameric structure of copper-containing nitrite reductase of an anammox bacterium KSU-1
Daisuke Hira1, Misa Matsumura1, Ryuji Kitamura1
1Department of Applied Life Science, Faculty of Biotechnology and Life Science, Sojo University, 4-22-1 Ikeda, Kumamoto, 860-0082, Japan.
Abstract:
Anaerobic ammonium oxidation (anammox) and denitrification are two different microbial reactions that form nitrogen gas. The initial step in the anammox reaction-reduction of nitrite to nitric oxide-is thought to be catalyzed by homologs of dissimilatory nitrite reductase, which is known to be involved in denitrification. Here, we reveal the crystal structure of the copper-containing nitrite reductase (CuNIR) of strain KSU-1, an anammox bacterium. CuNIR had a unique homohexameric structure with three disulfide bridges between homotrimers, although the trimer was similar to that of known CuNIRs. Kinetic and mutagenesis analyses suggested that the hexameric structure is important for the electron transfer reaction.
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