메뉴 건너뛰기




Volumn 580, Issue 5, 2006, Pages 1350-1354

A tyrosine residue deprotonates during oxygen reduction by the caa3 reductase from Rhodothermus marinus

Author keywords

Bacteriorhodopsin; Cytochrome c oxidase; Electron transfer; FTIR; Glutamic acid; Membrane; Proton translocation; Respiration; Tyrosine; Vibrational spectroscopy

Indexed keywords

BACTERIAL ENZYME; GLUTAMIC ACID; OXIDOREDUCTASE; OXYGEN; TYROSINE; WATER;

EID: 32344451238     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2006.01.055     Document Type: Article
Times cited : (21)

References (18)
  • 2
    • 1942504686 scopus 로고    scopus 로고
    • Proton pathways, ligand binding and dynamics of the catalytic site in haem-copper oxygen reductases: A comparison between the three families
    • M.M. Pereira, and M. Teixeira Proton pathways, ligand binding and dynamics of the catalytic site in haem-copper oxygen reductases: a comparison between the three families Biochim. Biophys. Acta 1655 2004 340 346
    • (2004) Biochim. Biophys. Acta , vol.1655 , pp. 340-346
    • Pereira, M.M.1    Teixeira, M.2
  • 3
    • 0034732961 scopus 로고    scopus 로고
    • The caa(3) terminal oxidase of Rhodothermus marinus lacking the key glutamate of the D-channel is a proton pump
    • M.M. Pereira, M.L. Verkhovskaya, M. Teixeira, and M.I. Verkhovsky The caa(3) terminal oxidase of Rhodothermus marinus lacking the key glutamate of the D-channel is a proton pump Biochemistry 39 2000 6336 6340
    • (2000) Biochemistry , vol.39 , pp. 6336-6340
    • Pereira, M.M.1    Verkhovskaya, M.L.2    Teixeira, M.3    Verkhovsky, M.I.4
  • 4
    • 1542298196 scopus 로고    scopus 로고
    • Investigation of protonatable residues in Rhodothermus marinus caa3 haem-copper oxygen reductase: Comparison with Paracoccus denitrificans aa3 haem-copper oxygen reductase
    • C.M. Soares, A.M. Baptista, M.M. Pereira, and M. Teixeira Investigation of protonatable residues in Rhodothermus marinus caa3 haem-copper oxygen reductase: comparison with Paracoccus denitrificans aa3 haem-copper oxygen reductase J. Biol. Inorg. Chem. 9 2004 124 134
    • (2004) J. Biol. Inorg. Chem. , vol.9 , pp. 124-134
    • Soares, C.M.1    Baptista, A.M.2    Pereira, M.M.3    Teixeira, M.4
  • 5
    • 0042307434 scopus 로고    scopus 로고
    • Direct observation of protonation reactions during the catalytic cycle of cytochrome c oxidase
    • R.M. Nyquist, D. Heitbrink, C. Bolwien, R.B. Gennis, and J. Heberle Direct observation of protonation reactions during the catalytic cycle of cytochrome c oxidase Proc. Natl. Acad. Sci. USA 100 2003 8715 8720
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 8715-8720
    • Nyquist, R.M.1    Heitbrink, D.2    Bolwien, C.3    Gennis, R.B.4    Heberle, J.5
  • 6
    • 8544253236 scopus 로고    scopus 로고
    • ATR-FTIR spectroscopy and isotope labeling of the PM intermediate of Paracoccus denitrificans cytochrome c oxidase
    • M. Iwaki, A. Puustinen, M. Wikstrom, and P.R. Rich ATR-FTIR spectroscopy and isotope labeling of the PM intermediate of Paracoccus denitrificans cytochrome c oxidase Biochemistry 43 2004 14370 14378
    • (2004) Biochemistry , vol.43 , pp. 14370-14378
    • Iwaki, M.1    Puustinen, A.2    Wikstrom, M.3    Rich, P.R.4
  • 7
    • 0033604850 scopus 로고    scopus 로고
    • Membrane-bound electron transfer chain of the thermohalophilic bacterium Rhodothermus marinus: A novel multihemic cytochrome bc, a new complex III
    • M.M. Pereira, J.N. Carita, and M. Teixeira Membrane-bound electron transfer chain of the thermohalophilic bacterium Rhodothermus marinus: a novel multihemic cytochrome bc, a new complex III Biochemistry 38 1999 1268 1275
    • (1999) Biochemistry , vol.38 , pp. 1268-1275
    • Pereira, M.M.1    Carita, J.N.2    Teixeira, M.3
  • 10
    • 0019878443 scopus 로고
    • Interactions of cytochrome aa3 with oxygen and carbon monoxide. the role of the 607 nm complex
    • P. Nicholls, and G.A. Chanady Interactions of cytochrome aa3 with oxygen and carbon monoxide. The role of the 607 nm complex Biochim. Biophys. Acta 634 1981 256 265
    • (1981) Biochim. Biophys. Acta , vol.634 , pp. 256-265
    • Nicholls, P.1    Chanady, G.A.2
  • 11
    • 3242708681 scopus 로고    scopus 로고
    • The molecular mechanism of membrane proteins probed by evanescent infrared waves
    • R.M. Nyquist, K. Ataka, and J. Heberle The molecular mechanism of membrane proteins probed by evanescent infrared waves Chembiochem 5 2004 431 436
    • (2004) Chembiochem , vol.5 , pp. 431-436
    • Nyquist, R.M.1    Ataka, K.2    Heberle, J.3
  • 12
    • 0037162391 scopus 로고    scopus 로고
    • Vibrational modes of tyrosines in cytochrome c oxidase from Paracoccus denitrificans: FTIR and electrochemical studies on Tyr-D4-labeled and on Tyr280His and Tyr35-Phe mutant enzymes
    • P. Hellwig, U. Pfitzner, J. Behr, B. Rost, R.P. Pesavento, W.V. Donk, R.B. Gennis, H. Michel, B. Ludwig, and W. Mäntele Vibrational modes of tyrosines in cytochrome c oxidase from Paracoccus denitrificans: FTIR and electrochemical studies on Tyr-D4-labeled and on Tyr280His and Tyr35-Phe mutant enzymes Biochemistry 41 2002 9116 9125
    • (2002) Biochemistry , vol.41 , pp. 9116-9125
    • Hellwig, P.1    Pfitzner, U.2    Behr, J.3    Rost, B.4    Pesavento, R.P.5    Donk, W.V.6    Gennis, R.B.7    Michel, H.8    Ludwig, B.9    Mäntele, W.10
  • 13
    • 0041846657 scopus 로고    scopus 로고
    • ATR-FTIR spectroscopy of the P(M) and F intermediates of bovine and Paracoccus denitrificans cytochrome c oxidase
    • M. Iwaki, A. Puustinen, M. Wikström, and P.R. Rich ATR-FTIR spectroscopy of the P(M) and F intermediates of bovine and Paracoccus denitrificans cytochrome c oxidase Biochemistry 42 2003 8809 8817
    • (2003) Biochemistry , vol.42 , pp. 8809-8817
    • Iwaki, M.1    Puustinen, A.2    Wikström, M.3    Rich, P.R.4
  • 14
    • 4644324308 scopus 로고    scopus 로고
    • Tyrosine 167: The origin of the radical species observed in the reaction of cytochrome c oxidase with hydrogen peroxide in Paracoccus denitrificans
    • K. Budiman, A. Kannt, S. Lyubenova, O.M. Richter, B. Ludwig, H. Michel, and F. MacMillan Tyrosine 167: the origin of the radical species observed in the reaction of cytochrome c oxidase with hydrogen peroxide in Paracoccus denitrificans Biochemistry 43 2004 11709 11716
    • (2004) Biochemistry , vol.43 , pp. 11709-11716
    • Budiman, K.1    Kannt, A.2    Lyubenova, S.3    Richter, O.M.4    Ludwig, B.5    Michel, H.6    MacMillan, F.7
  • 15
    • 0034673188 scopus 로고    scopus 로고
    • Functional properties of the heme propionates in cytochrome c oxidase from Paracoccus denitrificans. Evidence from FTIR difference spectroscopy and site-directed mutagenesis
    • J. Behr, H. Michel, W. Mäntele, and P. Hellwig Functional properties of the heme propionates in cytochrome c oxidase from Paracoccus denitrificans. Evidence from FTIR difference spectroscopy and site-directed mutagenesis Biochemistry 39 2000 1356 1363
    • (2000) Biochemistry , vol.39 , pp. 1356-1363
    • Behr, J.1    Michel, H.2    Mäntele, W.3    Hellwig, P.4
  • 16
    • 0027376991 scopus 로고
    • Comparative resonance Raman study of cytochrome c oxidase from beef heart and Paracoccus denitrificans
    • G.E. Heibel, P. Hildebrandt, B. Ludwig, P. Steinrucke, T. Soulimane, and G. Buse Comparative resonance Raman study of cytochrome c oxidase from beef heart and Paracoccus denitrificans Biochemistry 32 1993 10866 10877
    • (1993) Biochemistry , vol.32 , pp. 10866-10877
    • Heibel, G.E.1    Hildebrandt, P.2    Ludwig, B.3    Steinrucke, P.4    Soulimane, T.5    Buse, G.6
  • 17
    • 16344363592 scopus 로고    scopus 로고
    • Simulating redox coupled proton transfer in cytochrome c oxidase: Looking for the proton bottleneck
    • M.H. Olsson, P.K. Sharma, and A. Warshel Simulating redox coupled proton transfer in cytochrome c oxidase: looking for the proton bottleneck FEBS Lett. 579 2005 2026 2034
    • (2005) FEBS Lett. , vol.579 , pp. 2026-2034
    • Olsson, M.H.1    Sharma, P.K.2    Warshel, A.3
  • 18
    • 0036382724 scopus 로고    scopus 로고
    • The X-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides
    • M. Svensson-Ek, J. Abramson, G. Larsson, S. Tornroth, P. Brzezinski, and S. Iwata The X-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides J. Mol. Biol. 321 2002 329 339
    • (2002) J. Mol. Biol. , vol.321 , pp. 329-339
    • Svensson-Ek, M.1    Abramson, J.2    Larsson, G.3    Tornroth, S.4    Brzezinski, P.5    Iwata, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.