Pseudomonas aeruginosa nitrite

Shimada, H., and Orii, Y. (1976). Oxidation-reduction behavior of the heme c and heme d moieties of Pseudomonas aeruginosa nitrite reductase and the formation of an oxygenated intermediate at heme d. J. Biochem. (Tokyo) 80, 135-140. 

Sutherland, J., Greenwood, C., Peterson, J., and Thomson, A. J. (1986). An investigation of the ligand-binding properties of Pseudomonas aeruginosa nitrite reductase. Biochem. J. 233, 893-898. 

Pseudomonas aeruginosa nitrite reductase of, 274, 275 transhydrogenase of, 53 molecular properties, 57 purification, 54, 56... 

Direct electrochemistry has also been used (72-78) to couple the electrode reactions to enzymes for which the redox proteins act as cofactors. In the studies, the chemically reduced or oxidized enzyme was turned over through the use of a protein and its electrode reaction as the source or sink of electrons. In the first report (72, 73) of such application, the electrochemical reduction of horse heart cjd,ochrome c was coupled to the reduction of dioxygen in the presence of Pseudomonas aeruginosa nitrite reductase/cytochrome oxidase via the redox proteins, azurin and cytochrome C551. The system corresponded to an oxygen electrode in which the four-electron reduction of dioxygen was achieved relatively fast at pH 7. 

Cytochrome c-552 belongs to cytochrome c6 or c8 group. As the cytochromes of this group react rapidly with Pseudomonas aeruginosa nitrite reductase but does not react with cow cytochrome c oxidase (Yamanaka, 1992), their structures have been supposed to be similar to each other. Thus, their amino acid sequences resemble each other though the sequence of Chlorobium limicola f. thiosulfatophi-lum cytochrome c-555 shows smaller similarity to other cytochromes c6 or c8 than the similarities that other cytochromes c6 or c8 show each other (Table 3.2). 

Nagata Y, Yamanaka T, Okunuki K (1970) Amino acid composition and iV-terminus of Pseudomonas cytochrome oxidase (= Pseudomonas aeruginosa nitrite reductase). Biochim Biophys Acta 221 668-671... 

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... 

SUvestrini, M.C., S. FalcineUi, 1. Ciabatti, F. Culruzzola, and M. Brunori (1994). Pseudomonas aeruginosa nitrite reductase (or cytochrome oxidase) An overview. Biochimie 76, 641-654. 

Absorption spectra of oxidized and dithionite-reduced nitrite reductase from Pseudomonas aeruginosa. Solid line, oxidized enzyme dashed line, dithionite-reduced enzyme, in 40 mM potassium phosphate buffer, pH 6.9. The enzyme concentration was 8 fiM and the spectra were recorded at room temperature (20°C) under N in a Thunberg cuvette with a light-path of 1 cm. From Barber etal. (1976). 

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. 

Amarger, N., and Alexander, M. (1968). Nitrite formation from hydroxylamine and oximes by Pseudomonas aeruginosa. ]. Bacteriol. 95, 1651-1657. 

Kim, C.-H., and Hollocher, T. C. (1983). N tracer studies on the reduction of nitrite by the purified dissimilatory nitrite reductase of Pseudomonas aeruginosa.]. Biol. Chem. 258, 4861-4863. 

Silvestrini, M. C., Galeotti, C. L., Gervais, M., Schinina, E., Barra, D., Bossa, F., and Brunori, M. (1989). Nitrite reductase from Pseudomonas aeruginosa Sequence of the gene and protein. FEBS Lett. 254, 33-38. 

Several of these cytochromes use nitrogen compounds as electron acceptors. Cytochrome cdx from Pseudomonas aeruginosa is a greenish-brown soluble enzyme which contains one c and one chlorin dx) heme in each of two subunits of 63 000 molecular weight. The presence of four redox centres is appropriate for the efficient catalysis of the four-electron reduction of dioxygen to water. It appears, however, that its physiological role may be the reduction of nitrite to NO. Kinetic studies on the anaerobic reduction of cd, by Fe(EDTA)2- have focused attention on electron transfer between the heme groups in the enzyme.722... 

Bellelli A, Brzezinski P, Arese M, Cutruzzola F, Silvestrini MC, Brunori M. Electron transfer in zinc-reconstituted nitrite reductase from Pseudomonas aeruginosa. Biochem J 1996 319 407-10. 

Cutruzzola, F., Arese, M., Grasso, S., Bellelli, A., and Brunori, M., 1997, Tyrosine 10 in the c-haem domain is not involved in the catalytic mechanism of nitrite reductase from Pseudomonas aeruginosa, FEBS Lett. 412 3659369. 

Nurizzo, D., Silvestrini, M.-C., Mathieu, M., Cutruzzola, E., Bourgeois, D., E,fp, V., Hajdu, J., Brunori, M., Tegoni, M., and Cambillau, C., 1997, N-terminal arm exchange is observed in the 2.15 crystal structure of oxidised nitrite reductase from Pseudomonas aeruginosa. Structure 5 115791171. 

Yamanaka T, Ota A, Okunuki K (1961) A nitrite reducing system reconstituted with purified cytochrome components of Pseudomonas aeruginosa. Biochim Biophys Acta 53 294-308... 

C34H3oFeN40io, Mr 710.48 uv , (tetramethyl ester) 660,611,570,532,446,422 nm. H. d belongs to the structural class of the isobacteriochlorins. Occurrence H. d, is one of the two prosthetic groups of cytochrorae cdp Cytochrome cdj, and thus also H. d, participates in the reduction of nitrite to NjO in chemoautotrophic bacteria such as Pseudomonas aeruginosa, Paracoccus denitriflcans, and Thiobacil-lus denitriflcans. H. dj is isolated from such denitri-ficating bacteria, which play an important role in the global nitrogen cycle. 

Nitrite reduction to nitric oxide is catalyzed by dissimilatory nitrite reductase. The enzymes purified from Alcaligenes faecalis (Iwasaki and Matsub-ara, 1971), Pseudomonas aeruginosa (Walker and Nicholas, 1961), andMj-crococcus denitrificans (Newton, 1969) have been shown to contain c d-type cytochrome. The nitrite reductase from Achromobacter cycloclastes does not... 

Heme di (107), which was isolated by Timkovich et al (70) and Chang et al (71) occurs as one of two cofactors in the reductase cytochrome cd. Cytochrome cd participates in the reduction of nitrite to nitrous oxide (N2O) in chemoautotrophic bacteria, such as Pseudomonas aeruginosa, Paracoccus denitrificans, and Thiobacillus denitrificans (13). From recent investigations it seems very likely that cytochrome cdi mediates the nitrite reduction to nitric oxide (NO) and that a second enzyme produces N2O from NO (13). A structure was... 

---