메뉴 건너뛰기




Volumn 49, Issue 39, 2010, Pages 8546-8553

Enzymatic interconversion of ammonia and nitrite: The right tool for the job

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME C NITRITE REDUCTASE; DISPROPORTIONATIONS; ELECTRON REDUCTION; HYDROXYLAMINE OXIDOREDUCTASE; INTERCONVERSIONS; KINETIC DATA; METHYL VIOLOGEN; MONOCATIONS; NITROSOMONAS EUROPAEA; NUMBER OF ELECTRONS; OH CONCENTRATION; OXIDATIVE PROCESS; OXIDOREDUCTASES;

EID: 77957277232     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi1006783     Document Type: Article
Times cited : (36)

References (37)
  • 1
    • 1942475411 scopus 로고    scopus 로고
    • Physiologic and proteomic evidence for a role of nitric oxide in biofilm formation by Nitrosomonas europaea and other ammonia oxidizers
    • Schmidt, I., Steenbakkers, P. J. M., op den Camp, H. J. M., Schmidt, K., and Jetten, M. S. M. (2004) Physiologic and proteomic evidence for a role of nitric oxide in biofilm formation by Nitrosomonas europaea and other ammonia oxidizers J. Bacteriol. 186, 2781-2788
    • (2004) J. Bacteriol. , vol.186 , pp. 2781-2788
    • Schmidt, I.1    Steenbakkers, P.J.M.2    Op Den Camp, H.J.M.3    Schmidt, K.4    Jetten, M.S.M.5
  • 2
    • 0004222377 scopus 로고    scopus 로고
    • 4th ed., Marcel Dekker, Inc., New York.
    • Ehrlich, H. L. (2002) Geomicrobiology, 4th ed., Marcel Dekker, Inc., New York.
    • (2002) Geomicrobiology
    • Ehrlich, H.L.1
  • 3
    • 51849098544 scopus 로고    scopus 로고
    • Kinetic and product distribution analysis of NO reductase activity in Nitrosomonas europaea hydroxylamine oxidoreductase
    • Kostera, J., Youngblut, M. D., Slosarczyk, J. M., and Pacheco, A. A. (2008) Kinetic and product distribution analysis of NO reductase activity in Nitrosomonas europaea hydroxylamine oxidoreductase J. Biol. Inorg. Chem. 13, 1073-1083
    • (2008) J. Biol. Inorg. Chem. , vol.13 , pp. 1073-1083
    • Kostera, J.1    Youngblut, M.D.2    Slosarczyk, J.M.3    Pacheco, A.A.4
  • 4
    • 0030611275 scopus 로고    scopus 로고
    • The 2.8 angstrom structure of hydroxylamine oxidoreductase from a nitrifying chemoautotrophic bacterium, Nitrosomonas europaea
    • Igarashi, N., Moriyama, H., Fujiwara, T., Fukumori, Y., and Tanaka, N. (1997) The 2.8 angstrom structure of hydroxylamine oxidoreductase from a nitrifying chemoautotrophic bacterium, Nitrosomonas europaea Nat. Struct. Biol. 4, 276-284
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 276-284
    • Igarashi, N.1    Moriyama, H.2    Fujiwara, T.3    Fukumori, Y.4    Tanaka, N.5
  • 5
    • 0027197328 scopus 로고
    • Hydroxylamine Oxidoreductase from Nitrosomonas europaea Is a Multimer of an Octa-Heme Subunit
    • Arciero, D. M. and Hooper, A. B. (1993) Hydroxylamine Oxidoreductase from Nitrosomonas europaea Is a Multimer of an Octa-Heme Subunit J. Biol. Chem. 268, 14645-14654
    • (1993) J. Biol. Chem. , vol.268 , pp. 14645-14654
    • Arciero, D.M.1    Hooper, A.B.2
  • 6
    • 13644249873 scopus 로고    scopus 로고
    • Redox equilibria in hydroxylamine oxidoreductase. Electrostatic control of electron redistribution in multielectron oxidative processes
    • Kurnikov, I. V., Ratner, M. A., and Pacheco, A. A. (2005) Redox equilibria in hydroxylamine oxidoreductase. Electrostatic control of electron redistribution in multielectron oxidative processes Biochemistry 44, 1856-1863
    • (2005) Biochemistry , vol.44 , pp. 1856-1863
    • Kurnikov, I.V.1    Ratner, M.A.2    Pacheco, A.A.3
  • 8
    • 0034671914 scopus 로고    scopus 로고
    • Cytochrome c nitrite reductase from Wolinella succinogenes: Structure at 1.6 angstrom resolution, inhibitor binding, and heme-packing motifs
    • Einsle, O., Stach, P., Messerschmidt, A., Simon, J., Kroger, A., Huber, R., and Kroneck, P. M. H. (2000) Cytochrome c nitrite reductase from Wolinella succinogenes: Structure at 1.6 angstrom resolution, inhibitor binding, and heme-packing motifs J. Biol. Chem. 275, 39608-39616
    • (2000) J. Biol. Chem. , vol.275 , pp. 39608-39616
    • Einsle, O.1    Stach, P.2    Messerschmidt, A.3    Simon, J.4    Kroger, A.5    Huber, R.6    Kroneck, P.M.H.7
  • 10
    • 0037592981 scopus 로고    scopus 로고
    • Cytochrome c nitrite reductase from Desulfovibrio desulfuricans ATCC 27774: The relevance of the two calcium sites in the structure of the catalytic subunit (NrfA)
    • Cunha, C. A., Macieira, S., Dias, J. M., Almeida, G., Goncalves, L. L., Costa, C., Lampreia, J., Huber, R., Moura, J. J. G., Moura, I., and Romao, M. J. (2003) Cytochrome c nitrite reductase from Desulfovibrio desulfuricans ATCC 27774: The relevance of the two calcium sites in the structure of the catalytic subunit (NrfA) J. Biol. Chem. 278, 17455-17465
    • (2003) J. Biol. Chem. , vol.278 , pp. 17455-17465
    • Cunha, C.A.1    MacIeira, S.2    Dias, J.M.3    Almeida, G.4    Goncalves, L.L.5    Costa, C.6    Lampreia, J.7    Huber, R.8    Moura, J.J.G.9    Moura, I.10    Romao, M.J.11
  • 13
    • 0037467739 scopus 로고    scopus 로고
    • Selective One-Electron Reduction of Nitrosomonas europaea Hydroxylamine Oxidoreductase with Nitric Oxide
    • Cabail, M. Z. and Pacheco, A. A. (2003) Selective One-Electron Reduction of Nitrosomonas europaea Hydroxylamine Oxidoreductase with Nitric Oxide Inorg. Chem. 42, 270-272
    • (2003) Inorg. Chem. , vol.42 , pp. 270-272
    • Cabail, M.Z.1    Pacheco, A.A.2
  • 14
    • 0026315645 scopus 로고
    • Spectroscopic and Rapid Kinetic Studies of Reduction of Cytochrome-C554 by Hydroxylamine Oxidoreductase from Nitrosomonas europaea
    • Arciero, D. M., Balny, C., and Hooper, A. B. (1991) Spectroscopic and Rapid Kinetic Studies of Reduction of Cytochrome-C554 by Hydroxylamine Oxidoreductase from Nitrosomonas europaea Biochemistry 30, 11466-11472
    • (1991) Biochemistry , vol.30 , pp. 11466-11472
    • Arciero, D.M.1    Balny, C.2    Hooper, A.B.3
  • 17
    • 33846223322 scopus 로고    scopus 로고
    • Hydrogen peroxide oxidation by catalase-peroxidase follows a non-scrambling mechanism
    • Vlasits, J., Jakopitsch, C., Schwanninger, M., Holubar, P., and Obinger, C. (2007) Hydrogen peroxide oxidation by catalase-peroxidase follows a non-scrambling mechanism FEBS Lett. 581, 320-324
    • (2007) FEBS Lett. , vol.581 , pp. 320-324
    • Vlasits, J.1    Jakopitsch, C.2    Schwanninger, M.3    Holubar, P.4    Obinger, C.5
  • 18
    • 0001811208 scopus 로고
    • The Reaction of Nitrogen(II) Oxide with Diethylamine
    • Drago, R. S. and Paulik, F. E. (1960) The Reaction of Nitrogen(II) Oxide with Diethylamine J. Am. Chem. Soc. 82, 96-98
    • (1960) J. Am. Chem. Soc. , vol.82 , pp. 96-98
    • Drago, R.S.1    Paulik, F.E.2
  • 20
    • 0036936765 scopus 로고    scopus 로고
    • Pulsed ELDOR spectroscopy of the Mo(V)/Fe(III) state of sulfite oxidase prepared by one-electron reduction with Ti(III) citrate
    • Codd, R., Astashkin, A. V., Pacheco, A., Raitsimring, A. M., and Enemark, J. H. (2002) Pulsed ELDOR spectroscopy of the Mo(V)/Fe(III) state of sulfite oxidase prepared by one-electron reduction with Ti(III) citrate J. Biol. Inorg. Chem. 7, 338-350
    • (2002) J. Biol. Inorg. Chem. , vol.7 , pp. 338-350
    • Codd, R.1    Astashkin, A.V.2    Pacheco, A.3    Raitsimring, A.M.4    Enemark, J.H.5
  • 23
    • 0034663575 scopus 로고    scopus 로고
    • Electron transfer during the oxidation of ammonia by the chemolithotrophic bacterium Nitrosomonas europaea
    • Whittaker, M., Bergmann, D., Arciero, D., and Hooper, A. B. (2000) Electron transfer during the oxidation of ammonia by the chemolithotrophic bacterium Nitrosomonas europaea Biochim. Biophys. Acta 1459, 346-355
    • (2000) Biochim. Biophys. Acta , vol.1459 , pp. 346-355
    • Whittaker, M.1    Bergmann, D.2    Arciero, D.3    Hooper, A.B.4
  • 26
    • 0021763648 scopus 로고
    • Kinetics of reduction by substrate or dithionite and heme-heme electron transfer in the multiheme hydroxylamine oxidoreductase
    • Hooper, A. B., Tran, V. M., and Balny, C. (1984) Kinetics of reduction by substrate or dithionite and heme-heme electron transfer in the multiheme hydroxylamine oxidoreductase Eur. J. Biochem. 141, 565-571
    • (1984) Eur. J. Biochem. , vol.141 , pp. 565-571
    • Hooper, A.B.1    Tran, V.M.2    Balny, C.3
  • 27
    • 0017892709 scopus 로고
    • Hydroxylamine oxidoreductase from Nitrosomonas: Absorption spectra and content of heme and metal
    • Hooper, A. B., Maxwell, P. C., and Terry, K. R. (1978) Hydroxylamine oxidoreductase from Nitrosomonas: Absorption spectra and content of heme and metal Biochemistry 17, 2984-2989
    • (1978) Biochemistry , vol.17 , pp. 2984-2989
    • Hooper, A.B.1    Maxwell, P.C.2    Terry, K.R.3
  • 28
    • 0013807127 scopus 로고
    • Characterization of hydroxylamine-cytochrome c reductase from the chemoautotrohs Nitrosomonas europaea and Nitrosocystis oceanus
    • Hooper, A. B. and Nason, A. J. (1965) Characterization of hydroxylamine-cytochrome c reductase from the chemoautotrohs Nitrosomonas europaea and Nitrosocystis oceanus J. Biol. Chem. 240, 4044-4057
    • (1965) J. Biol. Chem. , vol.240 , pp. 4044-4057
    • Hooper, A.B.1    Nason, A.J.2
  • 30
    • 85068248349 scopus 로고    scopus 로고
    • Techniques for Investigating Hydroxylamine Disproportionation by Hydroxylamine Oxidoreductases
    • In (, Ed.) Academic Press, Inc., San Diego (in press).
    • Pacheco, A. A., McGarry, J. M., Kostera, J., and Corona, A. (2010) Techniques for Investigating Hydroxylamine Disproportionation by Hydroxylamine Oxidoreductases. In Methods in Enzymology (Klotz, M. G., Ed.) Academic Press, Inc., San Diego (in press).
    • (2010) Methods in Enzymology
    • Pacheco, A.A.1    McGarry, J.M.2    Kostera, J.3    Corona, A.4    Klotz, M.G.5
  • 32
    • 4243616042 scopus 로고
    • Principles of Structure, Bonding and Reactivity for Metal Nitrosyl Complexes
    • Enemark, J. H. and Feltham, R. D. (1974) Principles of Structure, Bonding and Reactivity for Metal Nitrosyl Complexes Coord. Chem. Rev. 13, 339-406
    • (1974) Coord. Chem. Rev. , vol.13 , pp. 339-406
    • Enemark, J.H.1    Feltham, R.D.2
  • 33
    • 0018654333 scopus 로고
    • Hydroxylamine oxidoreductase of nitrosomonas: Production of nitric oxide from hydroxylamine
    • Hooper, A. B. and Terry, K. R. (1979) Hydroxylamine oxidoreductase of nitrosomonas: Production of nitric oxide from hydroxylamine Biochim. Biophys. Acta 571, 12-20
    • (1979) Biochim. Biophys. Acta , vol.571 , pp. 12-20
    • Hooper, A.B.1    Terry, K.R.2
  • 34
    • 0345517351 scopus 로고    scopus 로고
    • + derivatives: Elusive nitrosyl ferric porphyrins
    • + derivatives: Elusive nitrosyl ferric porphyrins J. Am. Chem. Soc. 121, 5210-5219
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 5210-5219
    • Ellison, M.K.1    Scheidt, W.R.2
  • 35
    • 0036525942 scopus 로고    scopus 로고
    • Mechanistic aspects of the reactions of nitric oxide with transition-metal complexes
    • Ford, P. C. and Lorkovic, I. M. (2002) Mechanistic aspects of the reactions of nitric oxide with transition-metal complexes Chem. Rev. 102, 993-1017
    • (2002) Chem. Rev. , vol.102 , pp. 993-1017
    • Ford, P.C.1    Lorkovic, I.M.2
  • 36
    • 0037046164 scopus 로고    scopus 로고
    • Spectroscopic characterization of the NO adduct of hydroxylamine oxidoreductase
    • Hendrich, M. P., Upadhyay, A. K., Riga, J., Arciero, D. M., and Hooper, A. B. (2002) Spectroscopic characterization of the NO adduct of hydroxylamine oxidoreductase Biochemistry 41, 4603-4611
    • (2002) Biochemistry , vol.41 , pp. 4603-4611
    • Hendrich, M.P.1    Upadhyay, A.K.2    Riga, J.3    Arciero, D.M.4    Hooper, A.B.5
  • 37
    • 0034702817 scopus 로고    scopus 로고
    • Kinetics and equilibria in ligand binding by nitrophorins 1-4: Evidence for stabilization of a nitric oxide-ferriheme complex through a ligand-induced conformational trap
    • Andersen, J. F., Ding, X. D., Balfour, C., Shokhireva, T. K., Champagne, D. E., Walker, F. A., and Montfort, W. R. (2000) Kinetics and equilibria in ligand binding by nitrophorins 1-4: Evidence for stabilization of a nitric oxide-ferriheme complex through a ligand-induced conformational trap Biochemistry 39, 10118-10131
    • (2000) Biochemistry , vol.39 , pp. 10118-10131
    • Andersen, J.F.1    Ding, X.D.2    Balfour, C.3    Shokhireva, T.K.4    Champagne, D.E.5    Walker, F.A.6    Montfort, W.R.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.