Unique hexameric structure of copper-containing nitrite reductase of an anammox bacterium KSU-1.


Journal

Biochemical and biophysical research communications
ISSN: 1090-2104
Titre abrégé: Biochem Biophys Res Commun
Pays: United States
ID NLM: 0372516

Informations de publication

Date de publication:
04 06 2020
Historique:
received: 22 03 2020
accepted: 25 03 2020
pubmed: 7 4 2020
medline: 15 12 2020
entrez: 7 4 2020
Statut: ppublish

Résumé

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.

Identifiants

pubmed: 32248970
pii: S0006-291X(20)30641-0
doi: 10.1016/j.bbrc.2020.03.144
pii:
doi:

Substances chimiques

Bacterial Proteins 0
Nitrite Reductases EC 1.7.-
nitrite reductase, copper-containing EC 1.7.2.1

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

654-660

Informations de copyright

Copyright © 2020 Elsevier Inc. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.

Auteurs

Daisuke Hira (D)

Department of Applied Life Science, Faculty of Biotechnology and Life Science, Sojo University, 4-22-1 Ikeda, Kumamoto, 860-0082, Japan. Electronic address: hira@life.sojo-u.ac.jp.

Misa Matsumura (M)

Department of Applied Life Science, Faculty of Biotechnology and Life Science, Sojo University, 4-22-1 Ikeda, Kumamoto, 860-0082, Japan.

Ryuji Kitamura (R)

Department of Applied Life Science, Faculty of Biotechnology and Life Science, Sojo University, 4-22-1 Ikeda, Kumamoto, 860-0082, Japan.

Kenji Furukawa (K)

Graduate School of Science and Technology, Kumamoto University, 2-39-1 Kurokami, Kumamoto, 860-8555, Japan.

Takao Fujii (T)

Department of Applied Life Science, Faculty of Biotechnology and Life Science, Sojo University, 4-22-1 Ikeda, Kumamoto, 860-0082, Japan.

Articles similaires

Photosynthesis Ribulose-Bisphosphate Carboxylase Carbon Dioxide Molecular Dynamics Simulation Cyanobacteria
alpha-Synuclein Humans Animals Mice Lewy Body Disease

Two codependent routes lead to high-level MRSA.

Abimbola Feyisara Adedeji-Olulana, Katarzyna Wacnik, Lucia Lafage et al.
1.00
Methicillin-Resistant Staphylococcus aureus Penicillin-Binding Proteins Peptidoglycan Bacterial Proteins Anti-Bacterial Agents

Mutational analysis of Phanerochaete chrysosporium´s purine transporter.

Mariana Barraco-Vega, Manuel Sanguinetti, Gabriela da Rosa et al.
1.00
Phanerochaete Fungal Proteins Purines Aspergillus nidulans DNA Mutational Analysis

Classifications MeSH