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.

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Fungal nitric-oxide reductase (NOR) is a heme enzyme that catalyzes the reduction of NO to Nitric oxide (NO)1 serves as a messenger molecule for a variety of biological functions, including neurotransmission, vascular relaxation, and the inhibition of platelet aggregation. In mammalian systems, NO is generated from L-arginine and molecular oxygen (O 2 ), via catalysis by heme-enzyme nitricoxide synthase, whose crystal structure has recently been reported (1-3). Subsequently, the generated NO binds to the heme iron of soluble guanylate cyclase activating the conversion of GTP to cGMP. In addition, the crystal structures of the heme-based NO transport protein, nitrophorin, of a blood sucking insect were recently reported (4,5). NO is also a potential ligand (inhibitor) of many hemoproteins such as myoglobin, hemoglobin, and peroxidase (6 -8). Despite the close relation of NO to hemoproteins, only a small amount of structural information is available for NO adduct of hemoproteins. It is particularly noteworthy that much less is known concerning the ferric-NO (Fe 3ϩ -NO) complex of hemoproteins, and only one crystal structure of cytochrome c peroxidase by Poulos and co-workers (8, 9) and two of the ferric-porphyrin model compounds, Fe Fungal nitric oxide reductase (NOR), a heme enzyme, is involved in the denitrification process by the fungus Fusarium oxysporum (11). In this process, NO is produced from the reduction of NO 2 Ϫ catalyzed by nitrite reductase, which represents an additional NO generating biological system. In order to detoxify the generated NO, fungal NOR converts NO to N 2 O by the reaction (11),Based on spectroscopic and kinetic studies of this reaction, we proposed that the overall enzymatic reaction (Scheme 1) consists of three chemical reactions, Schemes 2-4 (12);

We determined the structure of the complex of the sensory histidine kinase (HK) and its cognate response regulator (RR) in the two-component signal transduction system of Thermotoga maritima. This was accomplished by fitting the high-resolution structures of the isolated HK domains and the RR onto the electron density map (3.8 A resolution) of the HK/RR complex crystal. Based on the structural information, we evaluated the roles of both interdomain and intermolecular interactions in the signal transduction of the cytosolic PAS-linked HK and RR system, in particular the O(2)-sensor FixL/FixJ system. The PAS-sensor domain of HK interacts with the catalytic domain of the same polypeptide chain by creating an interdomain beta sheet. The interaction site between HK and RR, which was confirmed by NMR, is suitable for the intermolecular transfer reaction of the phosphoryl group, indicating that the observed interaction is important for the phosphatase activity of HK that dephosphorylates phospho-RR.