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Crystal structure of nitric oxide reductase from denitrifying fungus Fusarium oxysporum

Nature Structural Biology volume 4, pages 827–832 (1997)Cite this article

Abstract

Structures of nitric oxide reductase (NOR) in the ferric resting and the ferrous CO states have been solved at 2.0 Å resolution. These structures provide significant new insights into how NO is reduced in biological systems. The haem distal pocket is open to solvent, implicating this region as a possible NADH binding site. In combination with mutagenesis results, a hydrogen-bonding network from the water molecule adjacent to the iron ligand to the protein surface of the distal pocket through the hydroxyl group of Ser 286 and the carboxyl group of Asp 393 can be assigned to a pathway for proton delivery during the NO reduction reaction.

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Authors and Affiliations

  1. The Institute of Physical and Chemical Research (RIKEN), Wako, Saitama, 351-01, Japan

    Sam-Yong Park, Shin-ichi Adachi, Hiro Nakamura, Tetsutaro lizuka & Yoshitsugu Shiro

  2. Gakushuin University, Mejiro, Toshima-ku, Tokyo, 170, Japan

    Hideaki Shimizu

  3. Division of Biological Sciences, Graduate School of Science, Hokkaido University, Sapporo, 060, Japan

    Atsushi Nakagawa & Isao Tanaka

  4. Institute of Applied Biochemistry, University of Tsukuba, Tsukuba, Ibaraki, 305, Japan

    Kazuhiko Nakahara & Hirofumi Shoun

  5. Department of Applied Chemistry, Chuo University, Bunkyo-ku, Tokyo, 112, Japan

    Eiji Obayashi

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  1. Sam-Yong Park
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Correspondence to Yoshitsugu Shiro.

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Park, SY., Shimizu, H., Adachi, Si. et al. Crystal structure of nitric oxide reductase from denitrifying fungus Fusarium oxysporum. Nat Struct Mol Biol 4, 827–832 (1997). https://doi.org/10.1038/nsb1097-827

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