메뉴 건너뛰기




Volumn 580, Issue 5, 2006, Pages 1345-1349

The role of tryptophan 272 in the Paracoccus denitrificans cytochrome c oxidase

Author keywords

Bioenergetics; Cytochrome c oxidase; Electron paramagnetic resonance spectroscopy; Tyrosine radical; Variants

Indexed keywords

CYTOCHROME C OXIDASE; HYDROGEN PEROXIDE; TRYPTOPHAN; TYROSINE;

EID: 32344448823     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2006.01.054     Document Type: Article
Times cited : (26)

References (23)
  • 1
    • 0034984506 scopus 로고    scopus 로고
    • Structures and proton-pumping strategies of mitochondrial respiratory enzymes
    • B.E. Schultz, and S.I. Chan Structures and proton-pumping strategies of mitochondrial respiratory enzymes Annu. Rev. Biophys. Biomol. Struct. 30 2001 23 65
    • (2001) Annu. Rev. Biophys. Biomol. Struct. , vol.30 , pp. 23-65
    • Schultz, B.E.1    Chan, S.I.2
  • 2
    • 0642283837 scopus 로고    scopus 로고
    • Cytochrome c oxidase - Structure, function, and physiology of a redox-driven molecular machine
    • O.-M.H. Richter, and B. Ludwig Cytochrome c oxidase - structure, function, and physiology of a redox-driven molecular machine Rev. Physiol. Biochem. Pharmacol. 147 2003 47 74
    • (2003) Rev. Physiol. Biochem. Pharmacol. , vol.147 , pp. 47-74
    • Richter, O.-M.H.1    Ludwig, B.2
  • 3
    • 0041765700 scopus 로고    scopus 로고
    • Redox-driven proton-pumping by hemecopper oxidases
    • P. Brzezinski, and G. Larsson Redox-driven proton-pumping by hemecopper oxidases Biochim. Biophys. Acta 1606 2003 1 13
    • (2003) Biochim. Biophys. Acta , vol.1606 , pp. 1-13
    • Brzezinski, P.1    Larsson, G.2
  • 4
    • 0028890031 scopus 로고
    • Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans
    • S. Iwata, C. Ostermeier, B. Ludwig, and H. Michel Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans Nature 376 1995 660 669
    • (1995) Nature , vol.376 , pp. 660-669
    • Iwata, S.1    Ostermeier, C.2    Ludwig, B.3    Michel, H.4
  • 6
    • 0030886203 scopus 로고    scopus 로고
    • Structure at 2.7 Å resolution of the Paracoccus denitrificans two-subunit cytochrome c oxidase complexed with an antibody Fv-fragment
    • C. Ostermeier, A. Harrenga, U. Ermler, and H. Michel Structure at 2.7 Å resolution of the Paracoccus denitrificans two-subunit cytochrome c oxidase complexed with an antibody Fv-fragment Proc. Natl. Acad. Sci. 94 1997 10547 10553
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 10547-10553
    • Ostermeier, C.1    Harrenga, A.2    Ermler, U.3    Michel, H.4
  • 7
    • 0026530174 scopus 로고
    • Oxygen activation and the conservation of energy in the cell
    • G.T. Babcock, and M. Wikström Oxygen activation and the conservation of energy in the cell Nature 356 1992 301 309
    • (1992) Nature , vol.356 , pp. 301-309
    • Babcock, G.T.1    Wikström, M.2
  • 9
    • 0033539479 scopus 로고    scopus 로고
    • Mass spectrometric determination of dioxygen bond splitting in the "peroxy" intermediate of cytochrome c oxidase
    • M. Fabian, W.W. Wong, R.B. Gennis, and G. Palmer Mass spectrometric determination of dioxygen bond splitting in the "peroxy" intermediate of cytochrome c oxidase Proc. Natl. Acad. Sci. USA 96 1999 13114 13117
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13114-13117
    • Fabian, M.1    Wong, W.W.2    Gennis, R.B.3    Palmer, G.4
  • 10
    • 0020490631 scopus 로고
    • Cytochrome c oxidase binding of hydrogen peroxide
    • D. Bickar, J. Bonaventura, and C. Bonaventura Cytochrome c oxidase binding of hydrogen peroxide Biochemistry 21 1982 2661 2666
    • (1982) Biochemistry , vol.21 , pp. 2661-2666
    • Bickar, D.1    Bonaventura, J.2    Bonaventura, C.3
  • 11
    • 0028851789 scopus 로고
    • The interaction of cytochrome oxidase with hydrogen peroxide: The relationship of compounds P and F
    • M. Fabian, and G. Palmer The interaction of cytochrome oxidase with hydrogen peroxide: the relationship of compounds P and F Biochemistry 34 1995 13802 13810
    • (1995) Biochemistry , vol.34 , pp. 13802-13810
    • Fabian, M.1    Palmer, G.2
  • 12
    • 0001805270 scopus 로고    scopus 로고
    • The reactions of hydrogen peroxide with bovine cytochrome c oxidase
    • S. Jünemann, P. Heathcote, and P.R. Rich The reactions of hydrogen peroxide with bovine cytochrome c oxidase Biochim. Biophys. Acta 1456 2000 56 66
    • (2000) Biochim. Biophys. Acta , vol.1456 , pp. 56-66
    • Jünemann, S.1    Heathcote, P.2    Rich, P.R.3
  • 13
    • 0033587483 scopus 로고    scopus 로고
    • Direct evidence for a tyrosine radical in the reaction of cytochrome c oxidase with hydrogen peroxide
    • F. MacMillan, A. Kannt, J. Behr, T. Prisner, and H. Michel Direct evidence for a tyrosine radical in the reaction of cytochrome c oxidase with hydrogen peroxide Biochemistry 38 1999 9179 9184
    • (1999) Biochemistry , vol.38 , pp. 9179-9184
    • MacMillan, F.1    Kannt, A.2    Behr, J.3    Prisner, T.4    Michel, H.5
  • 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.H. Richter, B. Ludiwg, 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.H.4    Ludiwg, B.5    Michel, H.6    MacMillan, F.7
  • 15
    • 1942472143 scopus 로고    scopus 로고
    • Tryptophan or tyrosine? on the nature of the amino acid radical formed following hydrogen peroxide treatment of cytochrome c oxidase
    • D.A. Svistunenko, M.T. Wilson, and C.E. Cooper Tryptophan or tyrosine? On the nature of the amino acid radical formed following hydrogen peroxide treatment of cytochrome c oxidase Biochim. Biophys. Acta 1655 2004 372 380
    • (2004) Biochim. Biophys. Acta , vol.1655 , pp. 372-380
    • Svistunenko, D.A.1    Wilson, M.T.2    Cooper, C.E.3
  • 16
    • 4544315704 scopus 로고    scopus 로고
    • An oxo-ferryl tryptophan radical catalytic intermediate in cytochrome c and quinol oxdiase trapped by microsecond freeze-hyperquenching (MHQ)
    • F.G.M. Wiertz, O.-M.H. Richter, A.V. Cherepanov, F. MacMillan, B. Ludiwg, and S. de Vries An oxo-ferryl tryptophan radical catalytic intermediate in cytochrome c and quinol oxdiase trapped by microsecond freeze-hyperquenching (MHQ) FEBS Lett. 575 2004 127 130
    • (2004) FEBS Lett. , vol.575 , pp. 127-130
    • Wiertz, F.G.M.1    Richter, O.-M.H.2    Cherepanov, A.V.3    MacMillan, F.4    Ludiwg, B.5    De Vries, S.6
  • 17
    • 0022821996 scopus 로고
    • Cytochrome c oxidase from Paracoccus denitrificans
    • B. Ludwig Cytochrome c oxidase from Paracoccus denitrificans Methods Enzymol. 126 1986 153 159
    • (1986) Methods Enzymol. , vol.126 , pp. 153-159
    • Ludwig, B.1
  • 18
    • 0028798287 scopus 로고
    • Engineered Fv fragments as a tool for the one-step purification of integral multisubunit membrane protein complexes
    • G. Kleymann, C. Ostermeier, B. Ludwig, A. Skerra, and H. Michel Engineered Fv fragments as a tool for the one-step purification of integral multisubunit membrane protein complexes Biotechnology (NY) 13 1995 155 160
    • (1995) Biotechnology (NY) , vol.13 , pp. 155-160
    • Kleymann, G.1    Ostermeier, C.2    Ludwig, B.3    Skerra, A.4    Michel, H.5
  • 19
    • 0032518436 scopus 로고    scopus 로고
    • Cytochrome-c-binding site on cytochrome oxidase in Paracoccus denitrificans
    • H. Witt, F. Malatesta, F. Nicoletti, M. Brunori, and B. Ludwig Cytochrome-c-binding site on cytochrome oxidase in Paracoccus denitrificans Eur. J. Biochem. 251 1998 367 373
    • (1998) Eur. J. Biochem. , vol.251 , pp. 367-373
    • Witt, H.1    Malatesta, F.2    Nicoletti, F.3    Brunori, M.4    Ludwig, B.5
  • 20
    • 1942536627 scopus 로고    scopus 로고
    • Important roles of tyrosines in Photosystem II and cytochrome oxidase
    • P.E.M. Siegbahn, and M.R.A. Blomberg Important roles of tyrosines in Photosystem II and cytochrome oxidase Biochim. Biophys. Acta 1655 2004 45 50
    • (2004) Biochim. Biophys. Acta , vol.1655 , pp. 45-50
    • Siegbahn, P.E.M.1    Blomberg, M.R.A.2
  • 21
    • 1942423697 scopus 로고    scopus 로고
    • Dynamic water networks in cytochrome c oxidase from Paracoccus denitrificans investigated by molecular dynamics simulations
    • E. Olkhova, M.C. Hutter, M.A. Lill, V. Helms, and H. Michel Dynamic water networks in cytochrome c oxidase from Paracoccus denitrificans investigated by molecular dynamics simulations Biophys. J. 86 2004 1873 1889
    • (2004) Biophys. J. , vol.86 , pp. 1873-1889
    • Olkhova, E.1    Hutter, M.C.2    Lill, M.A.3    Helms, V.4    Michel, H.5
  • 22
    • 0035371783 scopus 로고    scopus 로고
    • A novel scenario for the evolution of haem-copper oxygen reductases
    • M.M. Pereira, M. Santana, and M. Teixeira A novel scenario for the evolution of haem-copper oxygen reductases Biochim. Biophys. Acta 1505 2001 185 208
    • (2001) Biochim. Biophys. Acta , vol.1505 , pp. 185-208
    • Pereira, M.M.1    Santana, M.2    Teixeira, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.