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Volumn 1757, Issue 9-10, 2006, Pages 1110-1116

Proton pumping mechanism of bovine heart cytochrome c oxidase

Author keywords

Cytochrome c oxidase; Electron transfer; Heme protein; Membrane protein; O2 reduction; Proton pump; Site directed mutagenesis; X ray crystallography

Indexed keywords

AMINO ACID; CARBOXYL GROUP; COPPER; CYTOCHROME C OXIDASE; HEME; MEMBRANE PROTEIN; PROTON PUMP;

EID: 33748965935     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2006.06.004     Document Type: Review
Times cited : (62)

References (26)
  • 1
    • 0028813330 scopus 로고
    • Towards an understanding of the chemistry of oxygen reduction and proton translation in the iron-copper respiratory oxidases
    • Rich P.R. Towards an understanding of the chemistry of oxygen reduction and proton translation in the iron-copper respiratory oxidases. Aust. J. Plant Physiol. 22 (1995) 479-486
    • (1995) Aust. J. Plant Physiol. , vol.22 , pp. 479-486
    • Rich, P.R.1
  • 2
    • 0029150334 scopus 로고
    • Purpose of proton pathways
    • Wiliams R.J.P. Purpose of proton pathways. Nature 376 (1995) 643
    • (1995) Nature , vol.376 , pp. 643
    • Wiliams, R.J.P.1
  • 4
    • 0028890031 scopus 로고
    • Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans
    • Iwata S., Ostermeier C., Ludwig B., and Michel H. 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
  • 7
    • 0025981255 scopus 로고
    • Uptake and release of protons during the reaction between cytochrome c oxidase and molecular oxygen: a flow-flash investigation
    • Oliveberg M., Hallen S., and Nilson T. Uptake and release of protons during the reaction between cytochrome c oxidase and molecular oxygen: a flow-flash investigation. Biochemistry 30 (1991) 436-440
    • (1991) Biochemistry , vol.30 , pp. 436-440
    • Oliveberg, M.1    Hallen, S.2    Nilson, T.3
  • 9
    • 0021099512 scopus 로고
    • Redox-linked hydrogen bond strength changes in cytochrome a: implications for a cytochrome oxidase proton pump
    • Babcock G.T., and Callahan P.M. Redox-linked hydrogen bond strength changes in cytochrome a: implications for a cytochrome oxidase proton pump. Biochemistry 22 (1983) 2314-2319
    • (1983) Biochemistry , vol.22 , pp. 2314-2319
    • Babcock, G.T.1    Callahan, P.M.2
  • 10
    • 0024522067 scopus 로고
    • Cytochrome c oxidase: evidence for interaction of water molecules with cytochrome a
    • Sasaroli M., Ching Y., Dasgupta S., and Rousseau D.L. Cytochrome c oxidase: evidence for interaction of water molecules with cytochrome a. Biochemistry 28 (1989) 3128-3132
    • (1989) Biochemistry , vol.28 , pp. 3128-3132
    • Sasaroli, M.1    Ching, Y.2    Dasgupta, S.3    Rousseau, D.L.4
  • 11
    • 0000540212 scopus 로고
    • Proton exchange in amides: surprises from simple systems
    • Perrin C.L. Proton exchange in amides: surprises from simple systems. Acc. Chem. Res. 22 (1989) 268-275
    • (1989) Acc. Chem. Res. , vol.22 , pp. 268-275
    • Perrin, C.L.1
  • 12
    • 33645774468 scopus 로고    scopus 로고
    • Electronic structures of polyglycine and active sites of cytochrome c oxidase
    • Kamiya K., Shiraishi K., and Oshiyama A. Electronic structures of polyglycine and active sites of cytochrome c oxidase. J. Phys, Soc. Japan 73 (2004) 3198-3208
    • (2004) J. Phys, Soc. Japan , vol.73 , pp. 3198-3208
    • Kamiya, K.1    Shiraishi, K.2    Oshiyama, A.3
  • 15
    • 24944511130 scopus 로고    scopus 로고
    • Cytochrome c oxidase as a calcium binding protein. Studies on the role of a conserved aspartate in Helices XI-XII cytoplasmic loop in cation binding
    • Kirichenko A.V., Pfitzner U., Ludwig B., Soares C.M., Vygodina T.V., and Konstantinov A.A. Cytochrome c oxidase as a calcium binding protein. Studies on the role of a conserved aspartate in Helices XI-XII cytoplasmic loop in cation binding. Biochemistry 44 (2005) 12391-12401
    • (2005) Biochemistry , vol.44 , pp. 12391-12401
    • Kirichenko, A.V.1    Pfitzner, U.2    Ludwig, B.3    Soares, C.M.4    Vygodina, T.V.5    Konstantinov, A.A.6
  • 16
    • 0031798637 scopus 로고    scopus 로고
    • Cytochrome c oxidase (Heme aa3) from Paracoccus denitrificans: analysis of mutation in putative proton channels of subunit I
    • Pfitzner U., Odenwald A., Ostermann T., Weingard L., Ludwig B., and Richter O.M. Cytochrome c oxidase (Heme aa3) from Paracoccus denitrificans: analysis of mutation in putative proton channels of subunit I. J. Bioenerg. Biomembr. 30 (1998) 89-97
    • (1998) J. Bioenerg. Biomembr. , vol.30 , pp. 89-97
    • Pfitzner, U.1    Odenwald, A.2    Ostermann, T.3    Weingard, L.4    Ludwig, B.5    Richter, O.M.6
  • 17
    • 0034696637 scopus 로고    scopus 로고
    • Mutations in the putative H-channel in the cytochrome c oxidase from Rhodobacter spheroids show that this channel is not important for proton conduction but reveal modulation of the properties of heme a
    • Lee H.-M., Das T.K., Rousseau D.L., Mills D., Ferguson-Miller S., and Gennis R.B. Mutations in the putative H-channel in the cytochrome c oxidase from Rhodobacter spheroids show that this channel is not important for proton conduction but reveal modulation of the properties of heme a. Biochemistry 39 (2000) 2989-2996
    • (2000) Biochemistry , vol.39 , pp. 2989-2996
    • Lee, H.-M.1    Das, T.K.2    Rousseau, D.L.3    Mills, D.4    Ferguson-Miller, S.5    Gennis, R.B.6
  • 18
    • 33748966217 scopus 로고    scopus 로고
    • Electron and proton transfer in the arginine-54-methionine mutant of cytochrome c oxidase from Paracoccus denitrificans
    • Jasaitis A., Backgren C., Morgan J.E., Puustinen A., Verkhovsky M.I., and Wikstrom M. Electron and proton transfer in the arginine-54-methionine mutant of cytochrome c oxidase from Paracoccus denitrificans. Biochemistry 39 (2000) 2989-2996
    • (2000) Biochemistry , vol.39 , pp. 2989-2996
    • Jasaitis, A.1    Backgren, C.2    Morgan, J.E.3    Puustinen, A.4    Verkhovsky, M.I.5    Wikstrom, M.6
  • 19
    • 23844453716 scopus 로고    scopus 로고
    • Is a third proton-conducting pathway operative in bacterial cytochrome c oxidase?
    • Salje J., Ludwig B., and Richter O.M. Is a third proton-conducting pathway operative in bacterial cytochrome c oxidase?. Biochem. Soc. Trans. 33 (2005) 829-831
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 829-831
    • Salje, J.1    Ludwig, B.2    Richter, O.M.3
  • 20
    • 24644471025 scopus 로고    scopus 로고
    • A mechanistic principle for proton pumping by cytochrome c oxidase
    • Faxén K., Gilderson G., Ädelroth P., and Brzezinski P. A mechanistic principle for proton pumping by cytochrome c oxidase. Nature 437 (2005) 286-289
    • (2005) Nature , vol.437 , pp. 286-289
    • Faxén, K.1    Gilderson, G.2    Ädelroth, P.3    Brzezinski, P.4
  • 21
    • 0035371783 scopus 로고    scopus 로고
    • A novel scenario for the evolution of haem-copper oxygen reductase
    • Pereira M.M., Santana M., and Teixiera M. A novel scenario for the evolution of haem-copper oxygen reductase. Biochim. Biophys. Acta 1505 (2001) 185-208
    • (2001) Biochim. Biophys. Acta , vol.1505 , pp. 185-208
    • Pereira, M.M.1    Santana, M.2    Teixiera, M.3
  • 23
    • 0034643820 scopus 로고    scopus 로고
    • Tracing the D-pathway in reconstituted site-directed mutants of cytochrome c oxidase from Paracoccus denitrificans
    • Pfitzner U., Hoffmeier K., Harrenga A., Kannt A., Michel H., Bamberg E., Richter H., and Ludwig B. Tracing the D-pathway in reconstituted site-directed mutants of cytochrome c oxidase from Paracoccus denitrificans. Biochemistry 39 (2000) 6756-6762
    • (2000) Biochemistry , vol.39 , pp. 6756-6762
    • Pfitzner, U.1    Hoffmeier, K.2    Harrenga, A.3    Kannt, A.4    Michel, H.5    Bamberg, E.6    Richter, H.7    Ludwig, B.8
  • 24
    • 0037069405 scopus 로고    scopus 로고
    • A mutation in subunit I of cytochrome oxidase from Rhodobacter sphaeroides. Result in an increase in steady-state activity but completely eliminates proton pumping
    • Pawate A.S., Morgan J., Namslauer A., Mills D., Brzezinski P., Ferguson-Miller S., and Gennis R.B. A mutation in subunit I of cytochrome oxidase from Rhodobacter sphaeroides. Result in an increase in steady-state activity but completely eliminates proton pumping. Biochemistry 41 (2002) 13417-13423
    • (2002) Biochemistry , vol.41 , pp. 13417-13423
    • Pawate, A.S.1    Morgan, J.2    Namslauer, A.3    Mills, D.4    Brzezinski, P.5    Ferguson-Miller, S.6    Gennis, R.B.7
  • 25
    • 0041765700 scopus 로고    scopus 로고
    • Redox-driven proton pumping by heme-copper oxidases
    • Brzezinski P., and Larsson G. Redox-driven proton pumping by heme-copper oxidases. Biochim. Biophys. Acta 1605 (2003) 1-13
    • (2003) Biochim. Biophys. Acta , vol.1605 , pp. 1-13
    • Brzezinski, P.1    Larsson, G.2
  • 26
    • 0346734127 scopus 로고    scopus 로고
    • Redox-coupled proton translocation in biological systems: proton shuttling in cytochrome c oxidase
    • Namslauer A., Pawate A.S., Gennis R.B., and Brzezinski P. Redox-coupled proton translocation in biological systems: proton shuttling in cytochrome c oxidase. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 15543-15547
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 15543-15547
    • Namslauer, A.1    Pawate, A.S.2    Gennis, R.B.3    Brzezinski, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.