Nitrogen nitrite reductase

Fe Cytochrome oxidase reduction of oxygen to water Cytochrome P-450 0-insertion from O2, and detoxification Cytochromes b and c electron transport in respiration and photosynthesis Cytochrome f photosynthetic electron transport Ferredoxin electron transport in photosynthesis and nitrogen fixation Iron-sulfur proteins electron transport in respiration and photosynthesis Nitrate and nitrite reductases reduction to ammonium... 

NITRILE HYDRATASE NITRILE HYDRATASE NITRITE REDUCTASE Nitrogen analogues of carbenes,... 

Nitrite reductases (NiRs)—enzymes found in several strains of denitrifying bacteria— catalyze the one-electron reduction of nitrite anion to nitric oxide (Equation 1). - In addition to the importance of this process in the global nitrogen cycle (Figure 1), further incentive for the study of the denitrification process is provided by its environmental impact, ranging from the production of NO as a pollutant and NjO as a potent greenhouse gas, to lake eutrophication due to farm runoff that contains high concentrations of nitrates and nitrites. 

The involvement of HA during bacterial conversion of nitrate to NH3 (known also as the nitrate ammonification phase of the nitrogen cycle) has been studied at the molecular level as part of an effort to delineate the mechanism of conversion of nitrite to NH3 by a group of multiheme cytochromes of bacterial origin. The overall reduction reaction is depicted in equation 3 for cytochrome c-nitrite reductase " ... 

Blom was the first to demonstrate, in 1928, the formation of HA by an unknown mixture of bacteria which utilized nitrate as their sole nitrogen source to produce ammonia , an observation substantiated by Lindsey and Rhines who generalized this reaction to a diverse set of microorganisms capable of producing NH3 by reduction of both nitrites and nitrates. The mechanism of the 6-electron reduction of nitrite to ammonia (i.e. conversion of the [N + 02] species to by bacterial cytochrome c nitrite reductase... 

Arrangement of subunits in nitrite reductase from Achromohacter cycloclastes. Domains are denoted D1 and D2, copper sites are shaded spheres, and Cu ligands are denoted by one-letter abbreviations C for cysteine sulfur and H for histidine imidazole nitrogen. From Fenderson et al. (1991). 

Bacterial assimilatory nitrate reductases have similar properties.86/86a In addition, many bacteria, including E. coli, are able to use nitrate ions as an oxidant for nitrate respiration under anaerobic conditions (Chapter 18). Tire dissimilatory nitrate reductases involved also contain molybdenum as well as Fe-S centers.85 Tire E. coli enzyme receives electrons from reduced quinones in the plasma membrane, passing them through cytochrome b, Fe-S centers, and molybdopterin to nitrate. The three-subunit aPy enzyme contains cytochrome b in one subunit, an Fe3S4 center as well as three Fe4S4 clusters in another, and the molybdenum cofactor in the third.87 Nitrate reduction to nitrite is also on the pathway of denitrification, which can lead to release of nitrogen as NO, NzO, and N2 by the action of dissimi-latory nitrite reductases. These enzymes873 have been discussed in Chapters 16 and 18. 

A denitrifying nitrite reductase from Achromobacter cycloclastes1533 and Ps. denitrificans1534 is a copper protein, containing two moles copper per mole of protein (molecular weight 69 000). This reduces nitrite to nitrogen monoxide. 

Similar mechanisms operate in the action of nitrate reductase and nitrite reductase. Both of these substances are produced from ammonia by oxidation. Plants and soil bacteria can reduce these compounds to provide ammonia for metabolism. The common agricultural fertilizer ammonium nitrate, NH4NO3, provides reduced nitrogen for plant growth directly, and by providing a substrate for nitrate reduction. NADH or NADPH is the electron donor for nitrate reductase, depending on the organism. 

This chapter focuses on the chemistry ofbiomimetic copper nitrosyl complexes relevant to the NO-copper interactions in proteins that are central players in dissimilatory nitrogen oxide reduction (denitrification). The current state of knowledge of NO-copper interactions in nitrite reductase, a key denitrifying enzyme, is briefly surveyed the syntheses, structures, and reactivity of copper nitrosyl model complexes prepared to date are presented and the insight these model studies provide into the mechanisms of denitrification and the structures of other copper protein nitrosyl intermediates are discussed. Emphasis is placed on analysis of the geometric features, electronic structures, and biomimetic reactivity with NO or NOf of the only structurally characterized copper nitrosyls, a dicopper(II) complex bridged by NO and a mononuclear tris(pyrazolyl)hydroborate complex having a Cu(I)-NO formulation. 

Treusch, A. H., Leininger, S., Kletzin, A., Schuster, S. C., iGenk, H. P., and Schleper, C. (2005). Novel genes for nitrite reductase and Amo-related proteins indicate a role of uncultivated meso-philic crenarchaeota in nitrogen cycling. Environmental Microbiology 7, 1985—1995. 

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