메뉴 건너뛰기




Volumn 46, Issue 26, 2007, Pages 7804-7810

The unusal redox centers of SoxXA, a novel c-type heme-enzyme essential for chemotrophic sulfur-oxidation of Paracoccus pantotrophus

Author keywords

[No Author keywords available]

Indexed keywords

HEMOPROTEIN SOXXA; HIGHLY ANISOTROPIC LOW-SPIN (HALS); PARACOCCUS PANTOTROPHUS; REDOX POTENTIAL;

EID: 34347345062     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi7003526     Document Type: Article
Times cited : (32)

References (28)
  • 1
    • 0031032795 scopus 로고    scopus 로고
    • Oxidative metabolism of inorganic sulfur compounds by bacteria
    • Kelly, D. P., Shergill, J. K., Lu, W. P., and Wood, A. P. (1997) Oxidative metabolism of inorganic sulfur compounds by bacteria, Antonie Van Leeuwenhoek 71, 95-107.
    • (1997) Antonie Van Leeuwenhoek , vol.71 , pp. 95-107
    • Kelly, D.P.1    Shergill, J.K.2    Lu, W.P.3    Wood, A.P.4
  • 2
    • 0035408581 scopus 로고    scopus 로고
    • Oxidation of reduced inorganic sulfur compounds by bacteria: Emergence of a common mechanism?
    • Friedrich, C. G., Rother, D., Bardischewsky, F., Quentmeier, A., and Fischer, J. (2001) Oxidation of reduced inorganic sulfur compounds by bacteria: Emergence of a common mechanism?, Appl. Environ. Microbiol. 67, 2873-2882.
    • (2001) Appl. Environ. Microbiol , vol.67 , pp. 2873-2882
    • Friedrich, C.G.1    Rother, D.2    Bardischewsky, F.3    Quentmeier, A.4    Fischer, J.5
  • 4
    • 0032943528 scopus 로고    scopus 로고
    • A reevaluation of the taxonomy of Paracoccus denitrificans and a proposal for the combination Paracoccus pantotrophus comb
    • Rainey, F. A., Kelly, D. P., Stackebrandt, E., Burghardt, J., Hiraishi, A., Katayama, Y., and Wood, A. P. (1999) A reevaluation of the taxonomy of Paracoccus denitrificans and a proposal for the combination Paracoccus pantotrophus comb. nov, Int. J. Syst. Bacteriol. 49, 645-651.
    • (1999) Int. J. Syst. Bacteriol , vol.49 , pp. 645-651
    • Rainey, F.A.1    Kelly, D.P.2    Stackebrandt, E.3    Burghardt, J.4    Hiraishi, A.5    Katayama, Y.6    Wood, A.P.7
  • 6
    • 0034932333 scopus 로고    scopus 로고
    • Novel genes of the sox gene cluster, mutagenesis of the flavoprotein SoxF, and evidence for a general sulfur-oxidizing system in Paracoccus pantotrophus GB17
    • Rother, D., Henrich, H. J., Quentmeier, A., Bardischewsky, F., and Friedrich, C. G. (2001) Novel genes of the sox gene cluster, mutagenesis of the flavoprotein SoxF, and evidence for a general sulfur-oxidizing system in Paracoccus pantotrophus GB17, J. Bacteriol. 183, 4499-4508.
    • (2001) J. Bacteriol , vol.183 , pp. 4499-4508
    • Rother, D.1    Henrich, H.J.2    Quentmeier, A.3    Bardischewsky, F.4    Friedrich, C.G.5
  • 7
    • 0035902915 scopus 로고    scopus 로고
    • The cysteine residue of the SoxY protein as the active site of protein-bound sulfur oxidation of Paracoccus pantotrophus GB17
    • Quentmeier, A., and Friedrich, C. G. (2001) The cysteine residue of the SoxY protein as the active site of protein-bound sulfur oxidation of Paracoccus pantotrophus GB17, FEBS Lett. 503, 168-172.
    • (2001) FEBS Lett , vol.503 , pp. 168-172
    • Quentmeier, A.1    Friedrich, C.G.2
  • 8
    • 0033976381 scopus 로고    scopus 로고
    • Characterization of a new type of sulfite dehydrogenase from Paracoccus pantotrophus GB17
    • Quentmeier, A., Kraft, R., Kostka, S., Klockenkamper, R., and Friedrich, C. G. (2000) Characterization of a new type of sulfite dehydrogenase from Paracoccus pantotrophus GB17, Arch. Microbiol. 173, 117-125.
    • (2000) Arch. Microbiol , vol.173 , pp. 117-125
    • Quentmeier, A.1    Kraft, R.2    Kostka, S.3    Klockenkamper, R.4    Friedrich, C.G.5
  • 9
    • 18244368975 scopus 로고    scopus 로고
    • Sulfur dehydrogenase of Paracoccus pantotrophus: The heme-2 domain of the molybdoprotein cytochrome c complex is dispensable for catalytic activity
    • Bardischewsky, F., Quentmeier, A., Rother, D., Hellwig, P., Kostka, S., and Friedrich, C. G. (2005) Sulfur dehydrogenase of Paracoccus pantotrophus: The heme-2 domain of the molybdoprotein cytochrome c complex is dispensable for catalytic activity, Biochemistry 44, 7024-7034.
    • (2005) Biochemistry , vol.44 , pp. 7024-7034
    • Bardischewsky, F.1    Quentmeier, A.2    Rother, D.3    Hellwig, P.4    Kostka, S.5    Friedrich, C.G.6
  • 10
    • 20444472906 scopus 로고    scopus 로고
    • Multifrequency EPR analysis of the dimanganese cluster of the putative sulfate thiohydrolase SoxB of Paracoccus pantotrophus
    • Epel, B., Schaefer, K. O., Quentmeier, A., Friedrich, C., and Lubitz, W. (2005) Multifrequency EPR analysis of the dimanganese cluster of the putative sulfate thiohydrolase SoxB of Paracoccus pantotrophus, J. Biol. Inorg. Chem. 10, 636-642.
    • (2005) J. Biol. Inorg. Chem , vol.10 , pp. 636-642
    • Epel, B.1    Schaefer, K.O.2    Quentmeier, A.3    Friedrich, C.4    Lubitz, W.5
  • 11
    • 0033927420 scopus 로고    scopus 로고
    • A soxA gene, encoding a diheme cytochrome c, and a sox locus, essential for sulfur oxidation in a new sulfur lithotrophic bacterium
    • Mukhopadhyaya, P. N., Deb, C., Lahiri, C., and Roy, P. (2000) A soxA gene, encoding a diheme cytochrome c, and a sox locus, essential for sulfur oxidation in a new sulfur lithotrophic bacterium, J. Bacteriol. 182, 4278-4287.
    • (2000) J. Bacteriol , vol.182 , pp. 4278-4287
    • Mukhopadhyaya, P.N.1    Deb, C.2    Lahiri, C.3    Roy, P.4
  • 12
    • 0034805616 scopus 로고    scopus 로고
    • Cytochrome complex essential for photosynthetic oxidation of both thiosulfate and sulfide in Rhodovulum sulfidophilum
    • Appia-Ayme, C., Little, P. J., Matsumoto, Y., Leech, A. P., and Berks, B. C. (2001) Cytochrome complex essential for photosynthetic oxidation of both thiosulfate and sulfide in Rhodovulum sulfidophilum, J. Bacteriol. 183, 6107-6118.
    • (2001) J. Bacteriol , vol.183 , pp. 6107-6118
    • Appia-Ayme, C.1    Little, P.J.2    Matsumoto, Y.3    Leech, A.P.4    Berks, B.C.5
  • 13
    • 0035807062 scopus 로고    scopus 로고
    • Novel heme ligation in a c-type cytochrome involved in thiosulfate oxidation: EPR and MCD of SoxAX from Rhodovulum sulfidophilum
    • Cheesman, M. R., Little, P. J., and Berks, B. C. (2001) Novel heme ligation in a c-type cytochrome involved in thiosulfate oxidation: EPR and MCD of SoxAX from Rhodovulum sulfidophilum, Biochemistry 40, 10562-10569.
    • (2001) Biochemistry , vol.40 , pp. 10562-10569
    • Cheesman, M.R.1    Little, P.J.2    Berks, B.C.3
  • 14
    • 28944451694 scopus 로고    scopus 로고
    • Structure of the cytochrome complex SoxXA of Paracoccus pantotrophus, a heme enzyme initiating chemotrophic sulfur oxidation
    • Dambe, T., Quentmeier, A., Rother, D., Friedrich, C., and Scheidig, A. J. (2005) Structure of the cytochrome complex SoxXA of Paracoccus pantotrophus, a heme enzyme initiating chemotrophic sulfur oxidation, J. Struct. Biol. 152, 229-234.
    • (2005) J. Struct. Biol , vol.152 , pp. 229-234
    • Dambe, T.1    Quentmeier, A.2    Rother, D.3    Friedrich, C.4    Scheidig, A.J.5
  • 16
    • 1342325440 scopus 로고    scopus 로고
    • Cytochrome c(551) from Starkeya novella - Characterization, spectroscopic properties, and phytogeny of a diheme protein of the SoxAX family
    • Kappler, U., Aguey-Zinsou, K. F., Hanson, G. R., Bernhardt, P. V., and Mcewan, A. G. (2004) Cytochrome c(551) from Starkeya novella - Characterization, spectroscopic properties, and phytogeny of a diheme protein of the SoxAX family, J. Biol. Chem. 279, 6252-6260.
    • (2004) J. Biol. Chem , vol.279 , pp. 6252-6260
    • Kappler, U.1    Aguey-Zinsou, K.F.2    Hanson, G.R.3    Bernhardt, P.V.4    Mcewan, A.G.5
  • 17
    • 0037194438 scopus 로고    scopus 로고
    • The cytochrome complex SoxXA of Paracoccus pantotrophus is produced in Escherichia coli and functional in the reconstituted sulfur-oxidizing enzyme system
    • Rother, D., and Friedrich, C. G. (2002) The cytochrome complex SoxXA of Paracoccus pantotrophus is produced in Escherichia coli and functional in the reconstituted sulfur-oxidizing enzyme system, Biochim. Biophys. Acta 1598, 65-73.
    • (2002) Biochim. Biophys. Acta , vol.1598 , pp. 65-73
    • Rother, D.1    Friedrich, C.G.2
  • 18
    • 0032546595 scopus 로고    scopus 로고
    • Involvement of glutamic acid 278 in the redox reaction of the cytochrome c oxidase from Paracoccus denitrificans investigated by FTIR spectroscopy
    • Hellwig, P., Behr, J., Ostermeier, C., Richter, O. M. H., Pfitzner, U., Odenwald, A., Ludwig, B., Michel, H., and Mantele, W. (1998) Involvement of glutamic acid 278 in the redox reaction of the cytochrome c oxidase from Paracoccus denitrificans investigated by FTIR spectroscopy, Biochemistry 37, 7390-7399.
    • (1998) Biochemistry , vol.37 , pp. 7390-7399
    • Hellwig, P.1    Behr, J.2    Ostermeier, C.3    Richter, O.M.H.4    Pfitzner, U.5    Odenwald, A.6    Ludwig, B.7    Michel, H.8    Mantele, W.9
  • 19
    • 0034609560 scopus 로고    scopus 로고
    • FT-IR spectroscopic characterization of NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli: Oxidation of FeS cluster N2 is coupled with the protonation of an aspartate or glutamate side chains
    • Hellwig, P., Scheide, D., Bungert, S., Mantele, W., and Friedrich, T. (2000) FT-IR spectroscopic characterization of NADH:ubiquinone oxidoreductase (complex I) from Escherichia coli: Oxidation of FeS cluster N2 is coupled with the protonation of an aspartate or glutamate side chains, Biochemistry 39, 10884-10891.
    • (2000) Biochemistry , vol.39 , pp. 10884-10891
    • Hellwig, P.1    Scheide, D.2    Bungert, S.3    Mantele, W.4    Friedrich, T.5
  • 20
    • 0033049059 scopus 로고    scopus 로고
    • Electrochemical and ultraviolet/visible/infrared spectroscopic analysis of heme a and a(3) redox reactions in the cytochrome c oxidase from Paracoccus denitrificans: Separation of heme a and a(3) contributions and assignment of vibrational modes
    • Hellwig, P., Grzybek, S., Behr, J., Ludwig, B., Michel, H., and Mantele, W. (1999) Electrochemical and ultraviolet/visible/infrared spectroscopic analysis of heme a and a(3) redox reactions in the cytochrome c oxidase from Paracoccus denitrificans: Separation of heme a and a(3) contributions and assignment of vibrational modes, Biochemistry 38, 1685-1694.
    • (1999) Biochemistry , vol.38 , pp. 1685-1694
    • Hellwig, P.1    Grzybek, S.2    Behr, J.3    Ludwig, B.4    Michel, H.5    Mantele, W.6
  • 21
    • 0025115245 scopus 로고
    • Redox-linked conformational-changes in proteins detected by a combination of infrared-spectroscopy and protein electrochemistry - Evaluation of the technique with cytochrome-c
    • Moss, D., Nabedryk, E., Breton, J., and Mantele, W. (1990) Redox-linked conformational-changes in proteins detected by a combination of infrared-spectroscopy and protein electrochemistry - Evaluation of the technique with cytochrome-c, Eur. J. Biochem. 187, 565-572.
    • (1990) Eur. J. Biochem , vol.187 , pp. 565-572
    • Moss, D.1    Nabedryk, E.2    Breton, J.3    Mantele, W.4
  • 22
    • 0017184389 scopus 로고
    • Rapid and sensitive method for quantitation of microgram quantities of protein utilizing principle of protein-dye binding
    • Bradford, M. M. (1976) Rapid and sensitive method for quantitation of microgram quantities of protein utilizing principle of protein-dye binding, Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 23
    • 0033464509 scopus 로고    scopus 로고
    • Magnetic spectroscopic (EPR, ESEEM, Mossbauer, MCD and NMR) studies of low-spin ferriheme centers and their corresponding heme proteins
    • Walker, F. A. (1999) Magnetic spectroscopic (EPR, ESEEM, Mossbauer, MCD and NMR) studies of low-spin ferriheme centers and their corresponding heme proteins, Coord. Chem. Rev. 186, 471-534.
    • (1999) Coord. Chem. Rev , vol.186 , pp. 471-534
    • Walker, F.A.1
  • 24
    • 0032855443 scopus 로고    scopus 로고
    • Characterization of a de novo designed heme protein by EPR and ENDOR spectroscopy
    • Fahnenschmidt, M., Rau, H. K., Bittl, R., Haehnel, W., and Lubitz, W. (1999) Characterization of a de novo designed heme protein by EPR and ENDOR spectroscopy, Chem.-Eur. J. 5, 2327-2334.
    • (1999) Chem.-Eur. J , vol.5 , pp. 2327-2334
    • Fahnenschmidt, M.1    Rau, H.K.2    Bittl, R.3    Haehnel, W.4    Lubitz, W.5
  • 25
    • 0000674986 scopus 로고    scopus 로고
    • Electron paramagnetic resonance and electron nuclear double resonance spectroscopy of a heme protein maquette
    • Fahnenschmidt, M., Bittl, R., Rau, H. K., Haehnel, W., and Lubitz, W. (2000) Electron paramagnetic resonance and electron nuclear double resonance spectroscopy of a heme protein maquette, Chem. Phys. Lett. 323, 329-339.
    • (2000) Chem. Phys. Lett , vol.323 , pp. 329-339
    • Fahnenschmidt, M.1    Bittl, R.2    Rau, H.K.3    Haehnel, W.4    Lubitz, W.5
  • 26
    • 0034814589 scopus 로고    scopus 로고
    • Characterization of de novo synthesized four-helix bundle proteins with metalloporphyrin cofactors
    • Fahnenschmidt, M., Bittl, R., Schlodder, E., Haehnel, W., and Lubitz, W. (2001) Characterization of de novo synthesized four-helix bundle proteins with metalloporphyrin cofactors, Phys. Chem. Chem. Phys. 3, 4082-4090.
    • (2001) Phys. Chem. Chem. Phys , vol.3 , pp. 4082-4090
    • Fahnenschmidt, M.1    Bittl, R.2    Schlodder, E.3    Haehnel, W.4    Lubitz, W.5
  • 27
    • 0006563441 scopus 로고    scopus 로고
    • Kadish, K. M, Van Caemelbecke, E, Gueletii, E, Fukuzumi, S, Miyamoto, K, Suenobu, T, Tabard, A, and Guilard, R, 1998 Kinetic and thermodynamic studies of iron(III) and iron(IV) sigma-bonded porphyrins. Formation and reactivity of, OEP)Fe(R, n, where OEP is the dianion of octaethylporphyrin (n, 0, 1, 2, 3) and R, C6H5, 3,4,5-C6F3H2, 2,4,6-C6F 3H2, C6F4H, or C6F 5, Inorg. Chem. 37, 1759-1766
    • 5, Inorg. Chem. 37, 1759-1766.
  • 28
    • 0028237753 scopus 로고
    • Free-radical repair by a novel perthiol - Reversible hydrogen-transfer and perthiyl radical formation
    • Everett, S. A., Folkes, L. K., Wardman, P., and Asmus, K. D. (1994) Free-radical repair by a novel perthiol - Reversible hydrogen-transfer and perthiyl radical formation, Free Radical Res. 20, 387-400.
    • (1994) Free Radical Res , vol.20 , pp. 387-400
    • Everett, S.A.1    Folkes, L.K.2    Wardman, P.3    Asmus, K.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.