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Nitrite reductase characterization

Mikami, B. and S. Ida (1989). Spinach ferredoxin-nitrite reductase Characterization of catalytic activity and interaction of the enzyme with substrates. J. Biochem. 105, 47-50. [Pg.182]

To provide a model for nitrite reductases72 Karlin and co-workers characterized a nitrite-bound complex (226) (r = 0.05)214 In an endeavor to model nitrite reductase activity, Tanaka and co-workers prepared a few mononuclear complexes (227) (r = 0.74)215 (228) (r = 0.82),216 (229) (r = 0.97),217 (230) (r = 0.16),217 (231) (r = 0.07),217 and (232) (r = 0.43 and r = 0.53)217 and studied the electrochemical reduction of N02A As a part of their activity on modeling heme-copper terminal oxidases, Holm and co-workers prepared complex (233) (r = 0.96).218 Using a sterically hindered tris(pyridylmethyl)amine, Canary et al. prepared a complex (234) (r=1.00), studied its redox behavior, and discussed various factors that may contribute to the difference (higher potential for the new complex) in the redox potential of a Cu Cu1 couple between substituted and unsubstituted ligands.2 9... [Pg.783]

Since HA is unstable in vivo , and is known to rapidly associate with the heme part of heme proteins , and possibly also with a variety of biological oxidants, such as the superoxide anion that is produced by many mammalian cells, it is difficult to demonstrate its accumulation in vivo. Already in 1932 Lindsey and Rhines discussed some analytical difficulties in the detection of HA, since when added externally, it disappeared rapidly from bacterial cultures this led to the conclusion that even if it is produced as an intermediate, its consumption is too fast to allow the accumulation of sufficient quantities for analytical demonstration. Compelling indirect evidence for the presence of HA as an intermediate in the enzymatically catalyzed reduction of nitrite (N02 ) to NH3 was provided by Einsle and colleagues , who characterized the crystal structure of the complex obtained by soaking cytochrome c-nitrite reductase with NH20H. ... [Pg.612]

The work of Ye et al. (1991) was extended to include Tn5 mutants in nir genes for nitrite reductase of Pseudomonas fluorescens (Ye etal., 1992a) and Pseudomonas sp. strain G-179 (Ye et al., 1992b) which use, respectively, the cytochrome cd - and Cu-type nitrite reductase. The five mutants of P. fluorescens characterized not only lacked nitrite reductase and N0/H20- 0 exchange activities, but also showed levels of nitric oxide reductase activity that were diminished roughly by a factor of two. The reason for the decrease in nitric oxide reductase activity of the mutants is not clear, but may represent a change in... [Pg.299]

Akey, C. E., Moffat, K., Wharton, D. C., and Edelstein, S. j. (1980). Characterization of crystals of a cytochrome oxidase (nitrite reductase) from Pseudomonas aeruginosa by X-ray diffraction and electron microscopy. . Mol. Biol. 136, 19-43. [Pg.329]

Krueger, R. J., and Siegel, L. M. (1982). Spinach siroheme enzymes Isolation and characterization of ferredoxin-sulfite reductase and comparison of properties with ferre-doxin-nitrite reductase. Biochemistry 21, 2892-2904. [Pg.337]

Masuko, M., Iwasaki, H., Sakurai, T., Suzuki, S., and Nakahara, A. (1984). Characterization of nitrite reductase from a denitrifier, Alcaligenes. sp. NCIB 11015. A novel copper protein. J. Biochem. (Tokyo) 96, 447-454. [Pg.338]

Miller, D. J., and Nicholas, D. J. D. (1985). Characterization of a soluble cytochrome oxide/nitrite reductase from Nitrosomoruis europaea. J. Gen. Microbiol. 131, 2851-... [Pg.338]

Smith, G. B., and Tiedje, J. M. (1992). Isolation and characterization of a nitrite reductase gene and its use as a probe for denitrifying bacteria. Appl. Environ. Microbiol. 58, 376-... [Pg.341]

Ye, R. W., Arunakumari, A., Averill, B. A., and Tiedje, J. M. (1992a). Mutants of Pseudomonas fluorescens deficient in dissimilatory nitrite reduction are also altered in nitric oxide reduction.). Bacterial. 174, 2560-2564-Ye, R. W., Averill, B. A., and Tiedje, J. M. (1992b). Characterization of Tn5 mutants deficient in dissimilatory nitrite reduction in Pseudomonas sp. strain G-179, which contains a copper nitrite reductase.). Bacteriol. 174, 6653-6658. [Pg.343]

Oelmuller, R., Schuster, C. Mohr, H. (1988). Physiological characterization of a plastidic signal required for nitrate-induced appearance of nitrate and nitrite reductases. Planta 174, 75-83. [Pg.74]

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. [Pg.203]

E. M. Maes, "Structural Characterization of Iron and Copper Active Sites by Resonance Raman Spectroscopy Nitrophorin, Nitrite Reductase, and Iron-Sulfur Proteins, PhD. Dissertation, University of Houston, 2000. [Pg.6365]

Ritchie GAF, Nicholas DJD (1972) Identification of sources of nitrous oxide produced by oxidative and reductive processes in Nitrosomonas europaea. Biochem J 126 1189-1191 Ritchie GAF, Nicholas DJD (1974) The partial characterization of purified nitrite reductase and hydroxylamine oxidase from Nitrosomonas europaea. Biochem J 138 471 180... [Pg.143]

Silvestrini MC, Tordi MG, Citro G, Vecchini P, Brunori M (1995) Monomeric Pseudomonas aeruginosa nitrite reductase preparation, characterization, and kinetic properties. J Inorg Biochem 57 169-181... [Pg.145]


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Nitrite reductase

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