Structural Basis of Biological N 2 O Generation by Bacterial Nitric Oxide Reductase

Author:

Hino Tomoya123,Matsumoto Yushi14,Nagano Shingo15,Sugimoto Hiroshi1,Fukumori Yoshihiro6,Murata Takeshi23,Iwata So237,Shiro Yoshitsugu1

Affiliation:

1. RIKEN SPring-8 Center, 1-1-1 Kouto, Sayo, Hyogo 679-5148, Japan.

2. Japan Science and Technology Agency, Exploratory Research for Advanced Technology, Human Receptor Crystallography Project, Yoshida-Konoe-cho, Sakyo-ku, Kyoto 606-8501, Japan.

3. Department of Cell Biology, Graduate School of Medicine, Kyoto University, Yoshida-Konoe-cho, Sakyo, Kyoto 606-8501, Japan.

4. Division of Protein Chemistry, Post-Genome Science Center, Medical Institute of Bioregulation, Kyushu University, Fukuoka 812-8552, Japan.

5. Department of Chemistry and Biotechnology, Graduate School of Engineering, Tottori University, Tottori 680-8552, Japan.

6. Graduate School of Natural Science and Technology, Kanazawa University, Kanazawa, Ishikawa 920-1192, Japan.

7. Division of Molecular Bioscience, Membrane Protein Crystallography Group, Imperial College London, Exhibition Road, London SW7 2AZ, UK.

Abstract

Dissecting Nitric Oxide Reductase Bacterial breakdown of nitrogen compounds in soil and the oceans provides the largest emission source of the greenhouse gas, nitrous oxide (N 2 O). A key enzyme in this process is nitric oxide reductase (NOR), which catalyzes the reduction of nitric oxide (NO) to N 2 O. Hino et al. (p. 1666 , published online 25 November; see the Perspective by Moënne-Loccoz and Fee ) now describe the crystal structure of NOR from Pseudomonas aeruginosa . Consistent with their evolutionary relatedness, the transmembrane region topology and arrangement of metal centers in NOR are similar to those in cytochrome oxidases, key enzymes in aerobic respiration.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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