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Nitrosomonas europaea cytochrome

The amino acid sequence of Nitrobacter winogradskyi cytochrome c [cytochrome c-550(s)] is more similar to those of human and horse cytochromes c than that of Nitrosomonas europaea cytochrome c (cytochrome c-552) (Table 3.4). Namely, N. winogradskyi seems to have appeared on Earth evolutionarily later than N. europaea, on the basis of the amino acid sequence of cytochrome c (Yamanaka and Fukumori, 1988). So it is expected that Earth might have been polluted by nitrous acid or nitrite in the period between the appearance of N. europaea and N. [Pg.40]

Cytochrome c oxidase of Acidithiobacillus ferrooxidans was previously called cytochrome a1( as it shows the a peak at 595 nm (Ingledew, 1982). However, as the oxidase purified from the bacterium has two heme A molecules and two copper atoms in the minimal functional unit and one of the two molecules of heme A combines with carbon monoxide, it is a cytochrome aa3-type cytochrome c oxidase although it has the a peak at 595 nm (Kai et al., 1992). It differs from the usual cytochrome aa3 in having only one molecule of heme A and one atom of copper in the minimal structural unit, which comprises one molecule each of three kinds of subunits (54 kDa, 21 kDa, 15 kDa) like Starkeya novella cytochrome c oxidase (Shoji et al., 1992). [The DNA study suggests the presence of four subunits with the molecular masses of 69, 28, 18 and 6.4 kDa (Appia-Ayme et al., 1999)]. The minimal functional unit of the A. ferrooxidans oxidase is a dimer of the minimal structural unit, and the dimer shows general properties of cytochrome ach except that the a peak is present at a wavelength shorter than 600 nm of the absorption spectrum. The oxidase resembles Nitrosomonas europaea cytochrome c oxidase (Yamazaki et al., 1985) (see pp. 25-26) in the position of the a peak of the absorption spectrum. [Pg.84]

Fujiwara T, Yamanaka T, Fukumori Y (1995) The amino acid sequence of Nitrosomonas europaea cytochrome c-552. Curr Microbiol 31 1-4... [Pg.132]

Numata M, Yamazaki T, Fukumori Y, Yamanaka T (1989) Some properties of Nitrosomonas europaea cytochrome c oxidase (giant hemoglobin of the gutless beard worm Oligobranchia mashikoi. Proc Natl Acad Sci USA 102 14521-14526... [Pg.141]

MiUer, D. J., and Wood, P. M. (1983). The soluble cytochrome oxidase of Nitrosomonas europaea. Journal of General Microbiology 129, 1645-1650. [Pg.254]

Arciero DM, Balny C, Hooper AB (1991) Spectroscopic and rapid kinetic studies of reduction of cytochrome c-554 by hydroxylamine oxidoreductase from Nitrosomonas europaea. Biochemistry 30 11466-11472... [Pg.126]

Dickerson RE, Timkovich RC (1975) Cytochromes c. In Boyer PD (ed) The enzymes, vol XI part A. Academic Press, New York, pp 397-547 Diekert G, Klee B, Thauer RK (1980) Nickel, a component of factor F43o from Methanobacterium thermoautotrophicum. Arch Microbiol 124 103-106 DiSpirito AA, Lipscomb JD, Hooper AB (1986) Cytochrome aa3 from Nitrosomonas europaea. J Biol Chem 261 17048-17056... [Pg.130]

Elstner EF, Staffer C, Heupel A (1975) Determination of superoxide free radical ion and hydrogen peroxide as products of photosynthetic oxygen reduction. Z Naturforsch 30c 53-57 Emmel T, Sand W, Konig WA, Bock E (1986) Evidence for the existence of a sulphur oxygenase in Sulfolobus brierleyi. J Gen Microbiol 132 3415-3420 Ensign SA, Hyman MR, Arp DJ (1993) In vitro activation of ammonia monooxygenase from Nitrosomonas europaea by copper. J Bacteriol 175 1971-1980 Erickson RH, Hooper AB (1972) Preliminary characterization of variant CO-binding heme protein from Nitrosomonas. Biochim Biophys Acta 275 231-244 Erickson RH, Hooper AB, Terry KR (1972) Solubilization and purification of cytochrome a, from Nitrosomonas. Biochim Biophys Acta 283 155-166 Evans MCW, Buchanan BB, Amon DI (1966) A new ferredoxin-dependent carbon reduction cycle in a photosynthetic bacterium. Proc Natl Acad Sci USA 55 928-934 Falk JE (1964) Porpyrins and metalloporphyrins. Elsevier, Amsterdam... [Pg.131]

Hooper AB (1968) A nitrite reducing enzyme from Nitrosomonas europaea. Preliminary characterization with hydroxylamine as electron donor. Biochim Biophys Acta 162 49-65 Hooper AB, Erickson RH, Terry KR (1972) Electron transport system of Nitrosomonas isolation of a membrane-envelope fraction. J Bacterid 110 430-438 Hooper AB, Nason A (1965) Characterization of hydroxylamine-cytochrome c reductase from the chemoautotrophs Nitrosomonas europaea and Nitrosocystis oceanus. J Biol Chem 240 4044-4057... [Pg.134]

Ishimoto M, Koyama J, Nagai Y (1954) Biochemical studies on sulfate-reducing bacteria IV. The cytochrome system of sulfate-reducing bacteria. J Biochem 41 763-770 Ivanovsky RN, Krasilnikova EN, Fal YI (1993) A pathway of the autotrophic C02 fixation in Chloroflexus aurantiacus. Arch Microbiol 159 257-264 Iverson TM, Arciero DM, Hooper AB, Rees DC (2001) High solution structures of the oxidized and reduced states of cytochrome c-554 from Nitrosomonas europaea. J Biol Inorg Chem 6 390-397... [Pg.135]

Juliette LY, Hyman MR, Arp DJ (1993) Mechanism-based inactivation of ammonia monooxygenase in Nitrosomonas europaea by allylsulfide. Appl Environ Microbiol 59 3728-3735 Kadenbach B (1983) Structure and evolution of the Atmungsferment cytochrome c oxidase. Angew Chem Int ed Engl 22 275-283... [Pg.135]

Miller DJ, Wood PM, Nicholas DJD (1984) Further characterization of cytochrome P-460 in Nitrosomonas europaea. J Gen Microbiol 130 3049-3054 Miller SL (1953) A production of amino acids under possible primitive Earth conditions. Science 117 528-529... [Pg.140]

Numata M (1989) Studies on hydroxylamine oxidation in Nitrosomonas europaea. Dissertation for Masters degree, Tokyo Institute of Technology Numata M, Saito T, Yamazaki T, Fukumori Y, Yamanaka T (1990) Cytochrome P-460 of Nitrosomonas europaea further purification and further characterization. J Biochem 108 1016-... [Pg.141]

Poth M, Focht DD (1985) 15N kinetic analysis of N20 production by Nitrosomonas europaea an examination nitrifier denitrification. Appl Environ Microbiol 49 1134-1141 Powell SJ, Prosser JI (1985) The effect of nitrapyrin and chloropicolinic acid on ammonium oxidation by Nitrosomonas europaea. FEMS Microbiol Lett 28 51-54 Prince RC, Hooper AB (1987) Resolution of the hemes of hydroxylamine oxidoreductase by redox potentiometry and electron spin resonance spectroscopy. Biochemistry 26 970-974 Probst I, Bruschi M, Pfennig N, LeGall J (1977) Cytochrome c-551.5(c7) from Desulfuromonas acetoxidans. Biochim Biophys Acta 460 58-64... [Pg.143]

Suzuki I, Chan CW, Takeuchi TL (1992) Oxidation of elemental sulfur to sulfite by Thiobacillus thiooxidans cells. Appl Environ Microbiol 58 3767-3769 Suzuki I, Dular U, Kwok S-C (1974) Ammonia or ammonium ion as substrate for oxidation by Nitrosomonas europaea cells and extracts. J Bacteriol 120 556-558 Suzuki I, Kwok S-C (1970) Cell-free ammonia oxidation by Nitrosomonas europaea effects of polyamines, Mg2+ and albumin. Biochem Biophys Res Commun 39 950-955 Suzuki I, Kwok S-C (1981) A potential resolution and reconstitution of the ammonia oxidizing system of Nitrosomonas europaea. Role of cytochrome c-554. Can J Biochem 59 484-488... [Pg.146]

Upadhyay AK, Hooper AB, Hendrich MP (2006) NO reductase activity of the tetraheme cytochrome c-554 of Nitrosomonas europaea. J Am Chem Soc 128 4330-4337 Valkova-Valchanova MB, Chan SHP (1994) Purification and characterization of two new c-type cytochromes involved in Fe2+ oxidation from Thiobacillus ferrooxidans. FEBS Lett 288 159-162... [Pg.148]

Yamanaka T, Sakano Y (1980) Oxidation of hydroxylamine to nitrite catalyzed by hydroxylamine oxidoreductase purified from Nitrosomonas europaea. Curr Microbiol 4 239-244 Yamanaka T, Shinra M (1974) Cytochrome c-552 and cytochrome c-554 derived from Nitrosomonas europaea purification, properties and their function. J Biochem 75 1265-1273 Yamanaka T, Shinra M, Takahashi K, Shibasaka M (1979b) Highly purified hydroxylamine oxidoreductase derived from Nitrosomonas europaea. J Biochem 86 1101-1108 Yamanaka T, Takenami S, Akiyama N, Okunuki K (1971) Purification and properties of cytochrome c-550 and cytochrome c-551 derived from the facultative chemoautotroph, Thiobacillus novellus. J Biochem 70 349-358... [Pg.151]

Yamazaki Takehiro, Oyanagi H, Fujiwara T, Fukumori Y (1995) Nitrite reductase from the magnetotactic bacterium Magnetospirillum magnetotacticum. A novel cytochrome cdt with Fe(II) nitrite oxidoreductase activity. Eur 1 Biochem 233 665-671 Yamazaki Takeshi, Fukumori Y, Yamanaka T (1985) Cytochrome at of Nitrosomonas europaea resembles aa3-type cytochrome c oxidase in many respects. Biochim Biophys Acta 810 174-183... [Pg.151]

Yamazaki Takeshi, Fukumori Y, Yamanaka T (1988) Catalytic properties of cytochrome c oxidase purified from Nitrosomonas europaea. J Biochem 103 499-503 Yano T (1992) The oxidation system of ferrous ion in Thiobacillus ferrooxidans. Dissertation for Ph.D. degree, Tokyo Institute of Technology, Tokyo Yano T, Fukumori Y, Yamanaka T (1991) The amino acid sequence of rusticyanin isolated from Thiobacillus ferrooxidans. FEBS Lett 288 159-162 Yaoi Y (1967) Comparison of the primary structures of cytochromes c from wild and respiration-deficient mutant yeasts. J Biochem 61 54—58... [Pg.151]

Fig. 28.20 Cytochrome c554 isolated from Nitrosomonas europaea the protein chain shown in a ribbon representation and the four haem units. The Fe- - Fe distances between haem units are 950 pm, 1220 pm and 920 pm. Fig. 28.20 Cytochrome c554 isolated from Nitrosomonas europaea the protein chain shown in a ribbon representation and the four haem units. The Fe- - Fe distances between haem units are 950 pm, 1220 pm and 920 pm.
There are two main types of NiRs involved in the reduction of nitrites, namely, the heme-containing cytochrome cdj NiR which was obtained and first purified from Thiosphaera pantotropha (261). The second kind of NiR is the copper-containing NiR which was first isolated from Alcaligenes xylosoxidans NCIB 11015, a bacterial isolated from a soil in Japan. Other Cu NiR have been isolated from, Achromohacter cycloclastes, Alcaligenes faecalis S-6, Bacillus halodenitrificans, Haloferax denitrificans, Nitrosomonas europaea, Pseudomonas aureofaciens, Rhodobacter sphaeroides, and Hyphomicrobium sp. (262 and references thereinj. In mammalian systems, nitrites are reduced by deoxyHb (263) and by ferrous myoglobin (264,265) to nitric oxide. In synthetic iron porphyrins. Ford and coworkers have demonstrated how nitrites inhibit the reductive nitrosylation process by forming ferric-nitrites species (266). [Pg.71]

Miller, D. J., and D. J. D. Nicholas. 1985. Characterization of a soluble cytochrome oxidase/nitrite reductase from Nitrosomonas europaea. J. Gen. Microbiol. 131 2851-2854. [Pg.198]

See other pages where Nitrosomonas europaea cytochrome is mentioned: [Pg.71]    [Pg.202]    [Pg.322]    [Pg.154]    [Pg.728]    [Pg.728]    [Pg.126]    [Pg.127]    [Pg.127]    [Pg.132]    [Pg.137]    [Pg.140]    [Pg.142]    [Pg.146]    [Pg.148]    [Pg.152]    [Pg.853]    [Pg.6873]    [Pg.986]    [Pg.132]    [Pg.1094]    [Pg.198]    [Pg.26]   
See also in sourсe #XX -- [ Pg.3 , Pg.19 , Pg.23 , Pg.24 , Pg.25 , Pg.26 , Pg.27 , Pg.40 ]



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Nitrosomonas europaea

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