2ROM

CRYSTAL STRUCTURE OF NITRIC REDUCTASE FROM DENITRIFYING FUNGUS FUSARIUM OXYSPORUM COMPLEX WITH CARBON MONOXIDE

Summary for 2ROM

• Entry DOI: 10.2210/pdb2rom/pdb
• Descriptor: CYTOCHROME P450, PROTOPORPHYRIN IX CONTAINING FE, CARBON MONOXIDE, ... (4 entities in total)
• Functional Keywords: nitric oxide reductase, cytochrome p450nor, oxidoreductase
• Biological source: Fusarium oxysporum
• Total number of polymer chains: 1
• Total formula weight: 45065.19

Authors

Park, S.-Y.,Nakagawa, A. (deposition date: 1997-03-24, release date: 1997-10-15, Last modification date: 2024-02-21)

Primary citation

Park, S.Y.,Shimizu, H.,Adachi, S.,Nakagawa, A.,Tanaka, I.,Nakahara, K.,Shoun, H.,Obayashi, E.,Nakamura, H.,Iizuka, T.,Shiro, Y.
Crystal structure of nitric oxide reductase from denitrifying fungus Fusarium oxysporum.
Nat.Struct.Biol., 4:827-832, 1997

PubMed Abstract: Structures of nitric oxide reductase (NOR) in the ferric resting and the ferrous CO states have been solved at 2.0 A 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.

PubMed: 9334748
DOI: 10.1038/nsb1097-827

Experimental method

X-RAY DIFFRACTION (2 Å)