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Volumn 49, Issue 33, 2010, Pages 7033-7039

Functional role of Thr-312 and Thr-315 in the proton-transfer pathway in ba 3 cytochrome c oxidase from thermus thermophilus

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; CYTOCHROME C OXIDASE; HEME-COPPER OXIDASE; LOW DEGREE; PROTON UPTAKE; SEQUENCE HOMOLOGY; THERMUS THERMOPHILUS; TIME CONSTANTS; TIME-RESOLVED; WILD TYPES;

EID: 77955692484     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi100749p     Document Type: Article
Times cited : (18)

References (25)
  • 2
    • 0035371783 scopus 로고    scopus 로고
    • A novel scenario for the evolution of haem-copper oxygen reductases
    • Pereira, M. M., Santana, M., and Teixeira, M. (2001) A novel scenario for the evolution of haem-copper oxygen reductases Biochim. Biophys. Acta 1505, 185-208
    • (2001) Biochim. Biophys. Acta , vol.1505 , pp. 185-208
    • Pereira, M.M.1    Santana, M.2    Teixeira, M.3
  • 4
    • 33749052047 scopus 로고    scopus 로고
    • Chance and design: Proton transfer in water, channels and bioenergetic proteins
    • Wraight, C. A. (2006) Chance and design: Proton transfer in water, channels and bioenergetic proteins Biochim. Biophys. Acta 1757, 886-912
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 886-912
    • Wraight, C.A.1
  • 5
    • 0031744648 scopus 로고    scopus 로고
    • Pathways of proton transfer in cytochrome c oxidase
    • Brzezinski, P. and Ädelroth, P. (1998) Pathways of proton transfer in cytochrome c oxidase J. Bioenerg. Biomembr. 30, 99-107
    • (1998) J. Bioenerg. Biomembr. , vol.30 , pp. 99-107
    • Brzezinski, P.1    Ädelroth, P.2
  • 6
    • 0030745897 scopus 로고    scopus 로고
    • The roles of the two proton input channels in cytochrome c oxidase from Rhodobacter sphaeroides probed by the effects of site-directed mutations on time-resolved electrogenic intraprotein proton transfer
    • Konstantinov, A. A., Siletsky, S., Mitchell, D., Kaulen, A., and Gennis, R. B. (1997) The roles of the two proton input channels in cytochrome c oxidase from Rhodobacter sphaeroides probed by the effects of site-directed mutations on time-resolved electrogenic intraprotein proton transfer Proc. Natl. Acad. Sci. U.S.A. 94, 9085-9090
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 9085-9090
    • Konstantinov, A.A.1    Siletsky, S.2    Mitchell, D.3    Kaulen, A.4    Gennis, R.B.5
  • 8
    • 70349493006 scopus 로고    scopus 로고
    • 3 oxygen reductase from Thermus thermophilus uses a single input channel for proton delivery to the active site and for proton pumping
    • 3 oxygen reductase from Thermus thermophilus uses a single input channel for proton delivery to the active site and for proton pumping Proc. Natl. Acad. Sci. U.S.A. 106, 16169-16173
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 16169-16173
    • Chang, H.Y.1    Hemp, J.2    Chen, Y.3    Fee, J.A.4    Gennis, R.B.5
  • 11
    • 0034489319 scopus 로고    scopus 로고
    • Integrity of Thermus thermophilus cytochrome c552 synthesized by Escherichia coli cells expressing the host-specific cytochrome c maturation genes, ccmABCDEFGH: Biochemical, spectral, and structural characterization of the recombinant protein
    • Fee, J. A., Chen, Y., Todaro, T. R., Bren, K. L., Patel, K. M., Hill, M. G., Gomez-Moran, E., Loehr, T. M., Ai, J., Thöny-Meyer, L., Williams, P. A., Stura, E., Sridhar, V., and McRee, D. E. (2000) Integrity of Thermus thermophilus cytochrome c552 synthesized by Escherichia coli cells expressing the host-specific cytochrome c maturation genes, ccmABCDEFGH: Biochemical, spectral, and structural characterization of the recombinant protein Protein Sci. 9, 2074-2084
    • (2000) Protein Sci. , vol.9 , pp. 2074-2084
    • Fee, J.A.1    Chen, Y.2    Todaro, T.R.3    Bren, K.L.4    Patel, K.M.5    Hill, M.G.6    Gomez-Moran, E.7    Loehr, T.M.8    Ai, J.9    Thöny-Meyer, L.10    Williams, P.A.11    Stura, E.12    Sridhar, V.13    McRee, D.E.14
  • 15
    • 0029775911 scopus 로고    scopus 로고
    • Observation and assignment of peroxy and ferryl intermediates in the reduction of dioxygen to water by cytochrome c oxidase
    • Morgan, J. E., Verkhovsky, M. I., and Wikström, M. (1996) Observation and assignment of peroxy and ferryl intermediates in the reduction of dioxygen to water by cytochrome c oxidase Biochemistry 35, 12235-12240
    • (1996) Biochemistry , vol.35 , pp. 12235-12240
    • Morgan, J.E.1    Verkhovsky, M.I.2    Wikström, M.3
  • 17
    • 0034663494 scopus 로고    scopus 로고
    • The role of the D-and K-pathways of proton transfer in the function of the haem-copper oxidases
    • Wikström, M., Jasaitis, A., Backgren, C., Puustinen, A., and Verkhovsky, M. I. (2000) The role of the D-and K-pathways of proton transfer in the function of the haem-copper oxidases Biochim. Biophys. Acta 1459, 514-520
    • (2000) Biochim. Biophys. Acta , vol.1459 , pp. 514-520
    • Wikström, M.1    Jasaitis, A.2    Backgren, C.3    Puustinen, A.4    Verkhovsky, M.I.5
  • 18
    • 0032562214 scopus 로고    scopus 로고
    • Role of the pathway through K(I-362) in proton transfer in cytochrome c oxidase from R. sphaeroides
    • Ädelroth, P., Gennis, R. B., and Brzezinski, P. (1998) Role of the pathway through K(I-362) in proton transfer in cytochrome c oxidase from R. sphaeroides Biochemistry 37, 2470-2476
    • (1998) Biochemistry , vol.37 , pp. 2470-2476
    • Ädelroth, P.1    Gennis, R.B.2    Brzezinski, P.3
  • 19
    • 0026498102 scopus 로고
    • Proton transfer during the reaction between fully reduced cytochrome c oxidase and dioxygen: PH and deuterium isotope effects
    • Hallén, S. and Nilsson, T. (1992) Proton transfer during the reaction between fully reduced cytochrome c oxidase and dioxygen: pH and deuterium isotope effects Biochemistry 31, 11853-11859
    • (1992) Biochemistry , vol.31 , pp. 11853-11859
    • Hallén, S.1    Nilsson, T.2
  • 20
    • 0034727649 scopus 로고    scopus 로고
    • Formation of the "peroxy" intermediate in cytochrome c oxidase is associated with internal proton/hydrogen transfer
    • Karpefors, M., Ädelroth, P., Namslauer, A., Zhen, Y., and Brzezinski, P. (2000) Formation of the "peroxy" intermediate in cytochrome c oxidase is associated with internal proton/hydrogen transfer Biochemistry 39, 14664-14669
    • (2000) Biochemistry , vol.39 , pp. 14664-14669
    • Karpefors, M.1    Ädelroth, P.2    Namslauer, A.3    Zhen, Y.4    Brzezinski, P.5
  • 21
    • 0032493345 scopus 로고    scopus 로고
    • Dioxygen activation and bond cleavage by mixed-valence cytochrome c oxidase
    • Proshlyakov, D. A., Pressler, M. A., and Babcock, G. T. (1998) Dioxygen activation and bond cleavage by mixed-valence cytochrome c oxidase Proc. Natl. Acad. Sci. U.S.A. 95, 8020-8025
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 8020-8025
    • Proshlyakov, D.A.1    Pressler, M.A.2    Babcock, G.T.3
  • 23
    • 0033602933 scopus 로고    scopus 로고
    • Aspartate-132 in cytochrome c oxidase from Rhodobacter sphaeroides is involved in a two-step proton transfer during oxo-ferryl formation
    • Smirnova, I. A., Ädelroth, P., Gennis, R. B., and Brzezinski, P. (1999) Aspartate-132 in cytochrome c oxidase from Rhodobacter sphaeroides is involved in a two-step proton transfer during oxo-ferryl formation Biochemistry 38, 6826-6833
    • (1999) Biochemistry , vol.38 , pp. 6826-6833
    • Smirnova, I.A.1    Ädelroth, P.2    Gennis, R.B.3    Brzezinski, P.4
  • 24
    • 24644471025 scopus 로고    scopus 로고
    • A mechanistic principle for proton pumping by cytochrome c oxidase
    • Faxén, K., Gilderson, G., Ädelroth, P., and Brzezinski, P. (2005) A mechanistic principle for proton pumping by cytochrome c oxidase Nature 437, 286-289
    • (2005) Nature , vol.437 , pp. 286-289
    • Faxén, K.1    Gilderson, G.2    Ädelroth, P.3    Brzezinski, P.4
  • 25
    • 0029036305 scopus 로고
    • Control of electron delivery to the oxygen reduction site of cytochrome c oxidase: A role for protons
    • Verkhovsky, M. I., Morgan, J. E., and Wikström, M. (1995) Control of electron delivery to the oxygen reduction site of cytochrome c oxidase: A role for protons Biochemistry 34, 7483-7491
    • (1995) Biochemistry , vol.34 , pp. 7483-7491
    • Verkhovsky, M.I.1    Morgan, J.E.2    Wikström, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.