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Volumn 120, Issue 1-2, 2014, Pages 181-196

Affinity and activity of non-native quinones at the QB site of bacterial photosynthetic reaction centers

Author keywords

Electron transfer; Low potential quinone; Redox potential; Type II reaction centers

Indexed keywords

BACTERIA (MICROORGANISMS); RHODOBACTER SPHAEROIDES;

EID: 84898773607     PISSN: 01668595     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11120-013-9850-1     Document Type: Article
Times cited : (6)

References (82)
  • 1
    • 0019769585 scopus 로고
    • 870 to quinones
    • 1:CAS:528:DyaL38XhslCisg%3D%3D 10.1016/0005-2728(81)90228-0
    • 870 to quinones. Biochim Biophys Acta 638:201-209
    • (1981) Biochim Biophys Acta , vol.638 , pp. 201-209
    • Arata, H.1    Parson, W.W.2
  • 2
    • 0021226111 scopus 로고
    • One- and two-electron reduction of hydroxy-1,4-naphthoquinone and hydroxy-9,10-anthraquinones. The role of internal hydrogen bonding and its bearing on the redox chemistry of the anthracycline antitumour quinones
    • 1:CAS:528:DyaL2MXhs1M%3D 6487650 10.1016/0304-4165(84)90138-7
    • Ashnagar A, Bruce M, Dutton PL, Prince R (1984) One- and two-electron reduction of hydroxy-1,4-naphthoquinone and hydroxy-9,10-anthraquinones. The role of internal hydrogen bonding and its bearing on the redox chemistry of the anthracycline antitumour quinones. Biochim Biophys Acta 801:351-359
    • (1984) Biochim Biophys Acta , vol.801 , pp. 351-359
    • Ashnagar, A.1    Bruce, M.2    Dutton, P.L.3    Prince, R.4
  • 3
    • 0019051168 scopus 로고
    • Structural requirements of quinone coenzymes for endogenous and dye-mediated coupled electron transport in bacterial photosynthesis
    • 1:CAS:528:DyaL3MXksVagsw%3D%3D 7217045 10.1007/BF00744677
    • Baccarini-Melandri A, Gabellini N, Melandri BA, Hurt E, Hauska G (1980) Structural requirements of quinone coenzymes for endogenous and dye-mediated coupled electron transport in bacterial photosynthesis. J Bioenerg Biomembr 12:95-110
    • (1980) J Bioenerg Biomembr , vol.12 , pp. 95-110
    • Baccarini-Melandri, A.1    Gabellini, N.2    Melandri, B.A.3    Hurt, E.4    Hauska, G.5
  • 4
    • 0018790974 scopus 로고
    • The involvement of iron and ubiquinone in electron transfer reactions mediated by reaction centers from photosynthetic bacteria
    • 1:CAS:528:DyaE1MXhsVylsLs%3D 311656 10.1016/0005-2728(79)90152-X
    • Blankenship RE, Parson WW (1979) The involvement of iron and ubiquinone in electron transfer reactions mediated by reaction centers from photosynthetic bacteria. Biochim Biophys Acta 545:429-444
    • (1979) Biochim Biophys Acta , vol.545 , pp. 429-444
    • Blankenship, R.E.1    Parson, W.W.2
  • 5
    • 0016305015 scopus 로고
    • Effects of extraction and replacement of ubiquinone upon the photochemical activity of reaction centres and chromatophores from Rhodopseudomonas sphaeroides
    • 1:CAS:528:DyaE2MXlsVeruw%3D%3D 4547199 10.1016/0014-5793(74)80877-X
    • Cogdell RJ, Brune DC, Clayton RK (1974) Effects of extraction and replacement of ubiquinone upon the photochemical activity of reaction centres and chromatophores from Rhodopseudomonas sphaeroides. FEBS Lett 45:344-347
    • (1974) FEBS Lett , vol.45 , pp. 344-347
    • Cogdell, R.J.1    Brune, D.C.2    Clayton, R.K.3
  • 7
    • 0036999722 scopus 로고    scopus 로고
    • Structure, dynamics, and energetics of the primary photochemistry of photosystem II of oxygenic photosynthesis
    • 1:CAS:528:DC%2BD38XlsVWhu78%3D 12221988 10.1146/annurev.arplant.53. 100301.135238
    • Diner BA, Rappaport F (2002) Structure, dynamics, and energetics of the primary photochemistry of photosystem II of oxygenic photosynthesis. Annu Rev Plant Biol 53:551-580
    • (2002) Annu Rev Plant Biol , vol.53 , pp. 551-580
    • Diner, B.A.1    Rappaport, F.2
  • 8
    • 48549110354 scopus 로고
    • Effect of inhibitors, redox state and isoprenoid chain length on the affinity of ubiquinone for the secondary acceptor binding site in the reaction centers of photosynthetic bacteria
    • 1:CAS:528:DyaL2cXlt1Ogtrg%3D 10.1016/0005-2728(84)90211-1
    • Diner BA, Schenck CC, DeVitry C (1984) Effect of inhibitors, redox state and isoprenoid chain length on the affinity of ubiquinone for the secondary acceptor binding site in the reaction centers of photosynthetic bacteria. Biochim Biophys Acta 766:9-20
    • (1984) Biochim Biophys Acta , vol.766 , pp. 9-20
    • Diner, B.A.1    Schenck, C.C.2    Devitry, C.3
  • 9
    • 0001230179 scopus 로고
    • The iron-quinone electron-acceptor complex of photosystem II
    • 1:CAS:528:DyaK3MXhvVajsrk%3D 10.1111/j.1399-3054.1991.tb08753.x
    • Diner BA, Petrouleas V, Wendoloski JJ (1991) The iron-quinone electron-acceptor complex of photosystem II. Physiol Plant 81:423-436
    • (1991) Physiol Plant , vol.81 , pp. 423-436
    • Diner, B.A.1    Petrouleas, V.2    Wendoloski, J.J.3
  • 10
    • 0016592897 scopus 로고
    • 2 and reaction center of Rhodopseudomonas sphaeroides Ga. Membranes. Extinction coefficients, content, half-reduction potentials, kinetics and electric field alterations
    • 1:CAS:528:DyaE2MXksFCrtbc%3D 237543 10.1016/0005-2728(75)90092-4
    • 2 and reaction center of Rhodopseudomonas sphaeroides Ga. membranes. Extinction coefficients, content, half-reduction potentials, kinetics and electric field alterations. Biochim Biophys Acta 387:536-556
    • (1975) Biochim Biophys Acta , vol.387 , pp. 536-556
    • Dutton, P.L.1    Petty, K.M.2    Bonner, H.S.3    Morse, S.D.4
  • 11
    • 0000204983 scopus 로고
    • Temperature dependence of the electric field modulation of electron-transfer rates: Charge recombination in photosynthetic reaction centers
    • 1:CAS:528:DyaK3sXis1eksLY%3D 10.1021/j100125a033
    • Franzen S, Boxer SG (1993) Temperature dependence of the electric field modulation of electron-transfer rates: charge recombination in photosynthetic reaction centers. J Phys Chem 97:6304-6318
    • (1993) J Phys Chem , vol.97 , pp. 6304-6318
    • Franzen, S.1    Boxer, S.G.2
  • 12
    • 0035976014 scopus 로고    scopus 로고
    • Structure of photosystem i
    • 1:CAS:528:DC%2BD3MXnvFCktb0%3D 11687205 10.1016/S0005-2728(01)00195-5
    • Fromme P, Jordan P, Krauß N (2001) Structure of photosystem I. Biochim Biophys Acta 1507:5-31
    • (2001) Biochim Biophys Acta , vol.1507 , pp. 5-31
    • Fromme, P.1    Jordan, P.2    Krauß, N.3
  • 13
    • 0024650666 scopus 로고
    • In photosynthetic reaction centers, the free energy difference for electron transfer between quinones bound at the primary and secondary quinone-binding sites governs the observed secondary site specificity
    • 1:CAS:528:DyaL1MXitV2nu7k%3D 286977 2649889 10.1073/pnas.86.8.2658
    • Giangiacomo KM, Dutton PL (1989) In photosynthetic reaction centers, the free energy difference for electron transfer between quinones bound at the primary and secondary quinone-binding sites governs the observed secondary site specificity. Proc Natl Acad Sci USA 86:2658-2662
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 2658-2662
    • Giangiacomo, K.M.1    Dutton, P.L.2
  • 14
    • 0030607107 scopus 로고    scopus 로고
    • Rapid isolation of bacterial photosynthetic reaction centers with an engineered poly-histidine tag
    • 10.1016/0005-2728(96)00091-6
    • Goldsmith JO, Boxer SG (1996) Rapid isolation of bacterial photosynthetic reaction centers with an engineered poly-histidine tag. Biochim Biophys Acta 1276:171-175
    • (1996) Biochim Biophys Acta , vol.1276 , pp. 171-175
    • Goldsmith, J.O.1    Boxer, S.G.2
  • 15
    • 0032578541 scopus 로고    scopus 로고
    • -• In bacterial reaction centers of Rhodobacter sphaeroides determined by a driving force assay
    • 1:CAS:528:DyaK1cXmsV2iu7Y%3D 21700 9751725 10.1073/pnas.95.20.11679
    • -• in bacterial reaction centers of Rhodobacter sphaeroides determined by a driving force assay. Proc Natl Acad Sci USA 95:11679-11684
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 11679-11684
    • Graige, M.S.1    Feher, G.2    Okamura, M.Y.3
  • 16
    • 0033621050 scopus 로고    scopus 로고
    • Observation of the protonated semiquinone intermediate in isolated reaction centers from Rhodobacter sphaeroides: Implications for the mechanism of electron and proton transfer in proteins
    • 1:CAS:528:DyaK1MXltVeitL8%3D 10471298 10.1021/bi990708u
    • Graige MS, Paddock ML, Feher G, Okamura MY (1999) Observation of the protonated semiquinone intermediate in isolated reaction centers from Rhodobacter sphaeroides: implications for the mechanism of electron and proton transfer in proteins. Biochemistry 38:11465-11473
    • (1999) Biochemistry , vol.38 , pp. 11465-11473
    • Graige, M.S.1    Paddock, M.L.2    Feher, G.3    Okamura, M.Y.4
  • 18
    • 0001773456 scopus 로고
    • Quinones as prosthetic groups in membrane electron-transfer proteins I: Systematic replacement of the primary ubiquinone of photochemical reaction centers with other quinones
    • B.L. Trumpower (eds) Academic Press New York
    • Gunner MR, Tiede DM, Prince RC, Dutton PL (1982) Quinones as prosthetic groups in membrane electron-transfer proteins I: systematic replacement of the primary ubiquinone of photochemical reaction centers with other quinones. In: Trumpower BL (ed) Function of quinones in energy conserving systems. Academic Press, New York, pp 265-269
    • (1982) Function of Quinones in Energy Conserving Systems , pp. 265-269
    • Gunner, M.R.1    Tiede, D.M.2    Prince, R.C.3    Dutton, P.L.4
  • 21
    • 33845374514 scopus 로고
    • A site and the oxidized bacteriochlorophyll dimer
    • 1:CAS:528:DyaL28XksFyisrw%3D 10.1021/j100407a054
    • A site and the oxidized bacteriochlorophyll dimer. J Phys Chem 90:3783-3795
    • (1986) J Phys Chem , vol.90 , pp. 3783-3795
    • Gunner, M.R.1    Robertson, D.E.2    Dutton, P.L.3
  • 22
    • 57049149598 scopus 로고    scopus 로고
    • Modification of quinone electrochemistry by the proteins in the biological electron transfer chains: Examples from photosynthetic reaction centers
    • 1:CAS:528:DC%2BD1cXhsVagtL3M 2746407 18979192 10.1007/s10863-008-9179-1
    • Gunner MR, Madeo J, Zhu Z (2008) Modification of quinone electrochemistry by the proteins in the biological electron transfer chains: examples from photosynthetic reaction centers. J Bioenerg Biomembr 40:509-519
    • (2008) J Bioenerg Biomembr , vol.40 , pp. 509-519
    • Gunner, M.R.1    Madeo, J.2    Zhu, Z.3
  • 23
    • 0036469776 scopus 로고    scopus 로고
    • Reaction centers: The structure and evolution of biological solar power
    • 1:CAS:528:DC%2BD38XhtlGjtbk%3D 11852245 10.1016/S0968-0004(01)02034-5
    • Heathcote P (2002) Reaction centers: the structure and evolution of biological solar power. Trends Biochem Sci 27:79-86
    • (2002) Trends Biochem Sci , vol.27 , pp. 79-86
    • Heathcote, P.1
  • 24
    • 33947476144 scopus 로고
    • Non-ionic-cationic micellar properties of dimethyldodecylamine oxide
    • 1:CAS:528:DyaF38Xltl2isw%3D%3D 10.1021/j100808a025
    • Herrmann KW (1962) Non-ionic-cationic micellar properties of dimethyldodecylamine oxide. J Phys Chem 66(1962):295-300
    • (1962) J Phys Chem , vol.66 , Issue.1962 , pp. 295-300
    • Herrmann, K.W.1
  • 26
    • 0346732319 scopus 로고    scopus 로고
    • Redox potential of quinones in both electron transfer branches of photosystem i
    • 1:CAS:528:DC%2BD3sXpvFCqt7s%3D 12972408 10.1074/jbc.M306434200
    • Ishikita H, Knapp EW (2003) Redox potential of quinones in both electron transfer branches of photosystem I. J Biol Chem 278:52002-52011
    • (2003) J Biol Chem , vol.278 , pp. 52002-52011
    • Ishikita, H.1    Knapp, E.W.2
  • 27
    • 0022365315 scopus 로고
    • Temperature and detection-wavelength dependence of the picosecond electron transfer kinetics measured in Rhodopseudomonas sphaeroides reaction centers. Resolution of new spectral and kinetic components in the primary charge separation process
    • 1:CAS:528:DyaL2MXmtFWnt74%3D 10.1016/0005-2728(85)90204-X
    • Kirmaier C, Holten D, Parson WW (1985) Temperature and detection-wavelength dependence of the picosecond electron transfer kinetics measured in Rhodopseudomonas sphaeroides reaction centers. Resolution of new spectral and kinetic components in the primary charge separation process. Biochim Biophys Acta 810:33-48
    • (1985) Biochim Biophys Acta , vol.810 , pp. 33-48
    • Kirmaier, C.1    Holten, D.2    Parson, W.W.3
  • 29
    • 0242494128 scopus 로고    scopus 로고
    • 6f complex of oxygenic photosynthesis: Tuning the cavity
    • 1:CAS:528:DC%2BD3sXos1Cms7c%3D 14526088 10.1126/science.1090165
    • 6f complex of oxygenic photosynthesis: tuning the cavity. Science 302:1009-1014
    • (2003) Science , vol.302 , pp. 1009-1014
    • Kurisu, G.1    Zhang, H.2    Smith, J.L.3    Cramer, W.A.4
  • 32
    • 0032311166 scopus 로고    scopus 로고
    • Ubiquinone reduction and protonation in photosynthetic reaction centres from Rhodopseudomonas viridis: X-ray structures and their functional implications
    • 1:CAS:528:DyaK1cXksFGqsr4%3D 10.1016/S0005-2728(98)00054-1
    • Lancaster CRD (1998) Ubiquinone reduction and protonation in photosynthetic reaction centres from Rhodopseudomonas viridis: X-ray structures and their functional implications. Biochim Biophys Acta 1365:143-150
    • (1998) Biochim Biophys Acta , vol.1365 , pp. 143-150
    • Lancaster, C.R.D.1
  • 33
    • 0032478280 scopus 로고    scopus 로고
    • - And the associated processes in Rhodobacter sphaeroides R-26 reaction centers
    • 1:CAS:528:DyaK1cXhtVyns78%3D 9485433 10.1021/bi971699x
    • - and the associated processes in Rhodobacter sphaeroides R-26 reaction centers. Biochemistry 37:2818-2829
    • (1998) Biochemistry , vol.37 , pp. 2818-2829
    • Li, J.1    Gilroy, D.2    Tiede, D.M.3    Gunner, M.R.4
  • 35
    • 0034720688 scopus 로고    scopus 로고
    • - In Rhodobacter sphaeroides reaction centers
    • 1:CAS:528:DC%2BD3cXjsFOrsbw%3D 10858293 10.1021/bi992591f
    • - in Rhodobacter sphaeroides reaction centers. Biochemistry 39:7445-7454
    • (2000) Biochemistry , vol.39 , pp. 7445-7454
    • Li, J.1    Takahashi, E.2    Gunner, M.R.3
  • 36
    • 4243933105 scopus 로고
    • Picosecond kinetics: Absorption studies of an iron porphyrin and bacteriopheophytin using a streak camera
    • 1:CAS:528:DyaL38XkvFWlug%3D%3D 10.1016/0009-2614(81)80334-X
    • Liang Y, Nagus DK, Hochstrasser RM, Gunner MR, Dutton PL (1981) Picosecond kinetics: absorption studies of an iron porphyrin and bacteriopheophytin using a streak camera. Chem Phys Lett 84:236-240
    • (1981) Chem Phys Lett , vol.84 , pp. 236-240
    • Liang, Y.1    Nagus, D.K.2    Hochstrasser, R.M.3    Gunner, M.R.4    Dutton, P.L.5
  • 37
    • 0014314730 scopus 로고
    • Primary photochemistry and electron transport in Rhodospirillum rubrum
    • 1:CAS:528:DyaF1cXksVWrtbc%3D 5690721 10.1021/bi00847a029
    • Loach PA, Sekura SL (1968) Primary photochemistry and electron transport in Rhodospirillum rubrum. Biochemistry 7:2642-2649
    • (1968) Biochemistry , vol.7 , pp. 2642-2649
    • Loach, P.A.1    Sekura, S.L.2
  • 38
    • 23944507024 scopus 로고    scopus 로고
    • A site in bacterial reaction centers
    • 1:CAS:528:DC%2BD2MXmsFCqtLo%3D 2727067 16101283 10.1021/bi050544j
    • A site in bacterial reaction centers. Biochemistry 44:10994-11004
    • (2005) Biochemistry , vol.44 , pp. 10994-11004
    • Madeo, J.1    Gunner, M.R.2
  • 39
    • 80055006037 scopus 로고    scopus 로고
    • A) site of photosynthetic bacterial reaction centers
    • 1:CAS:528:DC%2BC3MXht12ksbbI 3202297 21863833 10.1021/ja205811f
    • A) site of photosynthetic bacterial reaction centers. J Am Chem Soc 133:17375-17385
    • (2011) J Am Chem Soc , vol.133 , pp. 17375-17385
    • Madeo, J.1    Mihajlovic, M.2    Lazaridis, T.3    Gunner, M.R.4
  • 40
    • 0002735129 scopus 로고
    • - Reaction in isolated reaction centers from the photosynthetic bacterium Rhodopseudomonas sphaeroides
    • 1:CAS:528:DyaL2cXot12lsg%3D%3D 10.1016/0005-2728(84)90139-7
    • - reaction in isolated reaction centers from the photosynthetic bacterium Rhodopseudomonas sphaeroides. Biochim Biophys Acta 764:46-54
    • (1984) Biochim Biophys Acta , vol.764 , pp. 46-54
    • Mancino, L.J.1    Dean, D.P.2    Blankenship, R.E.3
  • 41
    • 0025095210 scopus 로고
    • Investigations on the influence of headgroup substitution and isoprene side-chain length in the function of primary and secondary quinones of bacterial reaction centers
    • 1:CAS:528:DyaK3cXhslGrsrc%3D 2404516 10.1016/0005-2728(90)90227-U
    • McComb JC, Stein RR, Wraight CA (1990) Investigations on the influence of headgroup substitution and isoprene side-chain length in the function of primary and secondary quinones of bacterial reaction centers. Biochim Biophys Acta 1015:156-171
    • (1990) Biochim Biophys Acta , vol.1015 , pp. 156-171
    • McComb, J.C.1    Stein, R.R.2    Wraight, C.A.3
  • 42
    • 0014674063 scopus 로고
    • On the nature of the free radical formed during the primary process of bacterial photosynthesis
    • 1:CAS:528:DyaF1MXnsFWluw%3D%3D 4303202 10.1016/0005-2728(69)90105-4
    • McElroy JD, Feher G, Mauzerall DC (1969) On the nature of the free radical formed during the primary process of bacterial photosynthesis. Biochim Biophys Acta 172:180-183
    • (1969) Biochim Biophys Acta , vol.172 , pp. 180-183
    • McElroy, J.D.1    Feher, G.2    Mauzerall, D.C.3
  • 44
    • 0016754421 scopus 로고
    • The protonmotive Q cycle: A general formulation
    • 1:CAS:528:DyaE28XislSjtg%3D%3D 1227927 10.1016/0014-5793(75)80359-0
    • Mitchell P (1975) The protonmotive Q cycle: a general formulation. FEBS Lett 59:137-139
    • (1975) FEBS Lett , vol.59 , pp. 137-139
    • Mitchell, P.1
  • 45
    • 0000312485 scopus 로고    scopus 로고
    • Vibrational spectrum and torsional potential of 2-methoxy-3-methyl-1,4- benzoquinone
    • 1:CAS:528:DyaK1MXktlSqsro%3D 10.1021/jp984800w
    • Nonella M, Boullais C, Mioskowski C, Nabedryk E, Breton J (1999) Vibrational spectrum and torsional potential of 2-methoxy-3-methyl-1,4- benzoquinone. J Phys Chem 103:6363-6370
    • (1999) J Phys Chem , vol.103 , pp. 6363-6370
    • Nonella, M.1    Boullais, C.2    Mioskowski, C.3    Nabedryk, E.4    Breton, J.5
  • 46
    • 0000178540 scopus 로고
    • The primary acceptor in bacterial photosynthesis: Obligatory role of ubiquinone in photoactive reaction centers of Rhodopseudomonas sphaeroides
    • 10.1073/pnas.72.9.3491
    • Okamura MY, Isaacson RA, Feher G (1975) The primary acceptor in bacterial photosynthesis: obligatory role of ubiquinone in photoactive reaction centers of Rhodopseudomonas sphaeroides. Proc Natl Acad Sci USA 72:3492-3496
    • (1975) Proc Natl Acad Sci USA , vol.72 , pp. 3492-3496
    • Okamura, M.Y.1    Isaacson, R.A.2    Feher, G.3
  • 47
    • 0034640331 scopus 로고    scopus 로고
    • Proton and electron transfer in bacterial reaction centers
    • 1:CAS:528:DC%2BD3cXjsV2js7w%3D 10812030 10.1016/S0005-2728(00)00065-7
    • Okamura MY, Paddock ML, Graige MS, Feher G (2000) Proton and electron transfer in bacterial reaction centers. Biochim Biophys Acta 1458:148-163
    • (2000) Biochim Biophys Acta , vol.1458 , pp. 148-163
    • Okamura, M.Y.1    Paddock, M.L.2    Graige, M.S.3    Feher, G.4
  • 48
    • 0242657390 scopus 로고    scopus 로고
    • Proton transfer pathways and mechanism in bacterial reaction centers
    • 1:CAS:528:DC%2BD3sXptVWgtb8%3D 14630317 10.1016/S0014-5793(03)01149-9
    • Paddock ML, Feher G, Okamura MY (2003) Proton transfer pathways and mechanism in bacterial reaction centers. FEBS Lett 555:45-50
    • (2003) FEBS Lett , vol.555 , pp. 45-50
    • Paddock, M.L.1    Feher, G.2    Okamura, M.Y.3
  • 49
    • 0001011327 scopus 로고
    • Electrochemistry of ubiquinones, menaquinones and plastoquinones in aprotic solvents
    • 1:CAS:528:DyaL3sXmtVahu7o%3D 10.1016/0014-5793(83)80981-8
    • Prince RC, Dutton PL, Bruce JM (1983) Electrochemistry of ubiquinones, menaquinones and plastoquinones in aprotic solvents. FEBS Lett 160:273-276
    • (1983) FEBS Lett , vol.160 , pp. 273-276
    • Prince, R.C.1    Dutton, P.L.2    Bruce, J.M.3
  • 50
    • 0012952155 scopus 로고
    • Structural influences on the electrochemistry of ubiquinone
    • C.H. Kim H. Tedeschi J. Diwan J. Salerno (eds) Plenum Publishing Corporation New York
    • Prince RC, Halbert TR, Upton TH (1988) Structural influences on the electrochemistry of ubiquinone. In: Kim CH, Tedeschi H, Diwan J, Salerno J (eds) Advances in membrane biochemistry and bioenergetics. Plenum Publishing Corporation, New York
    • (1988) Advances in Membrane Biochemistry and Bioenergetics
    • Prince, R.C.1    Halbert, T.R.2    Upton, T.H.3
  • 52
    • 1942504828 scopus 로고    scopus 로고
    • A in reaction centers from Rhodobacter sphaeroides: Contributions from the protein and protein-lipid (cardiolipin) interactions
    • 1:CAS:528:DC%2BD2cXjt1CgsLY%3D 15100021 10.1016/j.bbabio.2003.07.012
    • A in reaction centers from Rhodobacter sphaeroides: contributions from the protein and protein-lipid (cardiolipin) interactions. Biochim Biophys Acta 1655:93-101
    • (2004) Biochim Biophys Acta , vol.1655 , pp. 93-101
    • Rinyu, L.1    Martin, E.W.2    Takahashi, E.3    Maroti, P.4    Wraight, C.A.5
  • 53
    • 33749550607 scopus 로고    scopus 로고
    • Conservation of distantly related membrane proteins: Photosynthetic reaction centers share a common structural core
    • 1:CAS:528:DC%2BD28XhtFWgt7vJ 16887904 10.1093/molbev/msl079
    • Sadekar S, Raymond J, Blankenship RE (2006) Conservation of distantly related membrane proteins: photosynthetic reaction centers share a common structural core. Mol Biol Evol 23:2001-2007
    • (2006) Mol Biol Evol , vol.23 , pp. 2001-2007
    • Sadekar, S.1    Raymond, J.2    Blankenship, R.E.3
  • 54
    • 0035865881 scopus 로고    scopus 로고
    • 2- and 3-substituted 1,4-naphthoquinone derivatives as subversive substrates of trypanothione reductase and lipoamide dehydrogenase from Trypanosoma cruzi: Synthesis and correlation between redox cycling activities and in vitro cytotoxicity
    • 1:CAS:528:DC%2BD3MXjt1OltA%3D%3D 11170645 10.1021/jm001079l
    • Salmon-Chemin L, Buisine E, Yardley V, Kohler S, Bebreu M-A, Landry V, Sergheraert C, Croft SL, Srauth-Siegel L, Davioud-Carvet E (2001) 2- and 3-substituted 1,4-naphthoquinone derivatives as subversive substrates of trypanothione reductase and lipoamide dehydrogenase from Trypanosoma cruzi: synthesis and correlation between redox cycling activities and in vitro cytotoxicity. J Med Chem 44:548-565
    • (2001) J Med Chem , vol.44 , pp. 548-565
    • Salmon-Chemin, L.1    Buisine, E.2    Yardley, V.3    Kohler, S.4    Bebreu, M.-A.5    Landry, V.6    Sergheraert, C.7    Croft, S.L.8    Srauth-Siegel, L.9    Davioud-Carvet, E.10
  • 55
    • 0001385236 scopus 로고    scopus 로고
    • Temperature and free energy dependence of the direct charge recombination rate from the secondary quinone in bacterial reaction centers from Rhodobacter sphaeroides
    • 1:CAS:528:DC%2BD3cXhsFGgsbw%3D 10.1021/jp9939118
    • Schmid R, Labahn A (2000) Temperature and free energy dependence of the direct charge recombination rate from the secondary quinone in bacterial reaction centers from Rhodobacter sphaeroides. J Phys Chem B 104:2928-2936
    • (2000) J Phys Chem B , vol.104 , pp. 2928-2936
    • Schmid, R.1    Labahn, A.2
  • 56
    • 0003035415 scopus 로고
    • - Recombination kinetics in reaction centers from Rhodopseudomonas viridis: The effect of pH and temperature
    • 1:CAS:528:DyaL1MXltFagtrY%3D 10.1016/S0005-2728(89)80165-3
    • - recombination kinetics in reaction centers from Rhodopseudomonas viridis: the effect of pH and temperature. Biochim Biophys Acta 974:54-65
    • (1989) Biochim Biophys Acta , vol.974 , pp. 54-65
    • Sebban, P.1    Wraight, C.A.2
  • 57
    • 0023647477 scopus 로고
    • - State in reaction centers from Rhodopseudomonas viridis
    • 1:CAS:528:DyaL2sXlslakt70%3D 3651444 10.1016/0005-2728(87)90093-4
    • - state in reaction centers from Rhodopseudomonas viridis. Biochim Biophys Acta 893:409-425
    • (1987) Biochim Biophys Acta , vol.893 , pp. 409-425
    • Shopes, R.J.1    Wraight, C.A.2
  • 59
    • 0015514066 scopus 로고
    • Electron acceptors in reaction center preparations from photosynthetic bacteria
    • 1:CAS:528:DyaE38XkvFyrur4%3D 4627844 10.1016/0005-2728(72)90042-4
    • Slooten L (1972) Electron acceptors in reaction center preparations from photosynthetic bacteria. Biochim Biophys Acta 275:208-218
    • (1972) Biochim Biophys Acta , vol.275 , pp. 208-218
    • Slooten, L.1
  • 60
    • 0030904273 scopus 로고    scopus 로고
    • Light-induced structural changes in photosynthetic reaction center: Implications for mechanism of electron-proton transfer
    • 1:CAS:528:DyaK2sXivFOqtL4%3D 9115209 10.1126/science.276.5313.812
    • Stowell MHB, McPhillips TM, Rees DC, Soltis SM, Abresch E, Feher G (1997) Light-induced structural changes in photosynthetic reaction center: implications for mechanism of electron-proton transfer. Science 276:812-816
    • (1997) Science , vol.276 , pp. 812-816
    • Stowell, M.H.B.1    McPhillips, T.M.2    Rees, D.C.3    Soltis, S.M.4    Abresch, E.5    Feher, G.6
  • 62
    • 0025169243 scopus 로고
    • L213 in the proton transfer pathway to the secondary quinone of reaction centers from Rhodobacter sphaeroides
    • 1:CAS:528:DyaK3MXjvFeqsQ%3D%3D 10.1016/0005-2728(90)90100-I
    • L213 in the proton transfer pathway to the secondary quinone of reaction centers from Rhodobacter sphaeroides. Biochim Biophys Acta 1020:107-111
    • (1990) Biochim Biophys Acta , vol.1020 , pp. 107-111
    • Takahashi, E.1    Wraight, C.A.2
  • 64
    • 0029769668 scopus 로고    scopus 로고
    • Time-resolved electrochromism associated with the formation of quinone anions in the Rhodobacter sphaeroides R-26 reaction center
    • 1:CAS:528:DyaK28XksFyjuro%3D 8718867 10.1021/bi9605907
    • Tiede DM, Vazquez J, Cordova J, Marone AP (1996) Time-resolved electrochromism associated with the formation of quinone anions in the Rhodobacter sphaeroides R-26 reaction center. Biochemistry 35:10763-10775
    • (1996) Biochemistry , vol.35 , pp. 10763-10775
    • Tiede, D.M.1    Vazquez, J.2    Cordova, J.3    Marone, A.P.4
  • 65
    • 0027474062 scopus 로고
    • A site interactions in the photosynthetic reaction center protein
    • 1:CAS:528:DyaK3sXkt1CktL0%3D 46208 8464908 10.1073/pnas.90.7.2920
    • A site interactions in the photosynthetic reaction center protein. Proc Natl Acad Sci USA 90:2920-2924
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 2920-2924
    • Warncke, K.1    Dutton, P.L.2
  • 66
    • 0027336755 scopus 로고
    • A site redox cofactor structure on equilibrium binding, in situ electrochemistry, and electron-transfer performance in the photosynthetic reaction center protein
    • 1:CAS:528:DyaK3sXitlSgtLc%3D 8490022 10.1021/bi00069a011
    • A site redox cofactor structure on equilibrium binding, in situ electrochemistry, and electron-transfer performance in the photosynthetic reaction center protein. Biochemistry 32:4769-4779
    • (1993) Biochemistry , vol.32 , pp. 4769-4779
    • Warncke, K.1    Dutton, P.L.2
  • 67
    • 85099528561 scopus 로고
    • A site in reaction centers of Rhodopseudomonas sphaeroides R-26
    • J. Biggins (eds) Martinus Nijhoff Dordrecht
    • A site in reaction centers of Rhodopseudomonas sphaeroides R-26. In: Biggins J (ed) Progress in photosynthesis research. Martinus Nijhoff, Dordrecht, pp 217-220
    • (1987) Progress in Photosynthesis Research , pp. 217-220
    • Warncke, K.1    Gunner, M.R.2    Dutton, P.L.3
  • 69
    • 0022839827 scopus 로고
    • Primary structure of the reaction center from Rhodopseudomonas sphaeroides
    • 1:CAS:528:DyaL1cXhtVygsr8%3D 3329732 10.1002/prot.340010405
    • Williams JC, Steiner LA, Feher G (1986) Primary structure of the reaction center from Rhodopseudomonas sphaeroides. Proteins Struct Funct Genet 1:312-325
    • (1986) Proteins Struct Funct Genet , vol.1 , pp. 312-325
    • Williams, J.C.1    Steiner, L.A.2    Feher, G.3
  • 70
    • 0021741695 scopus 로고
    • Nanosecond fluorescence from isolated photosynthetic reaction centers from Rhodopseudomonas sphaeroides
    • 1:CAS:528:DyaL2MXktlSlug%3D%3D 6333897 10.1016/0005-2728(84)90205-6
    • Woodbury NWT, Parson WW (1984) Nanosecond fluorescence from isolated photosynthetic reaction centers from Rhodopseudomonas sphaeroides. Biochim Biophys Acta 767:345-361
    • (1984) Biochim Biophys Acta , vol.767 , pp. 345-361
    • Woodbury, N.W.T.1    Parson, W.W.2
  • 71
    • 0022295869 scopus 로고
    • Picosecond kinetics of the initial photochemical electron-transfer reaction in bacterial photosynthetic reaction centers
    • 1:CAS:528:DyaL28XhslOqsw%3D%3D 3879185 10.1021/bi00347a002
    • Woodbury NW, Becker M, Middendorf D, Parson WW (1985) Picosecond kinetics of the initial photochemical electron-transfer reaction in bacterial photosynthetic reaction centers. Biochemistry 24:7516-7521
    • (1985) Biochemistry , vol.24 , pp. 7516-7521
    • Woodbury, N.W.1    Becker, M.2    Middendorf, D.3    Parson, W.W.4
  • 72
    • 0023048040 scopus 로고
    • Radical-pair energetics and decay mechanisms in reaction center containing anthraquinones or benzoquinones in place of ubiquinone
    • 1:CAS:528:DyaL28XlsV2qtrg%3D 3524681 10.1016/0005-2728(86)90243-4
    • Woodbury NW, Parson WW, Gunner MR, Prince RC, Dutton PL (1986) Radical-pair energetics and decay mechanisms in reaction center containing anthraquinones or benzoquinones in place of ubiquinone. Biochim Biophys Acta 851:6-22
    • (1986) Biochim Biophys Acta , vol.851 , pp. 6-22
    • Woodbury, N.W.1    Parson, W.W.2    Gunner, M.R.3    Prince, R.C.4    Dutton, P.L.5
  • 73
    • 84995002675 scopus 로고
    • The role of quinones in bacterial photosynthesis
    • 1:CAS:528:DyaL3cXhsVeitbs%3D 10.1111/j.1751-1097.1979.tb07211.x
    • Wraight CA (1979) The role of quinones in bacterial photosynthesis. Photochem Photobiol 30:767-776
    • (1979) Photochem Photobiol , vol.30 , pp. 767-776
    • Wraight, C.A.1
  • 74
    • 1242347393 scopus 로고    scopus 로고
    • Proton and electron transfer in the acceptor quinone complex of photosynthetic reaction centers from Rhodobacter sphaeroides
    • 1:CAS:528:DC%2BD2cXhtFCku7o%3D 14766369 10.2741/1236
    • Wraight CA (2004) Proton and electron transfer in the acceptor quinone complex of photosynthetic reaction centers from Rhodobacter sphaeroides. Front Biosci 9:309-337
    • (2004) Front Biosci , vol.9 , pp. 309-337
    • Wraight, C.A.1
  • 75
    • 0015955715 scopus 로고
    • The absolute quantum efficiency of bacteriochlorophyll photoxidation in reaction centers
    • 10.1016/0005-2728(74)90009-7
    • Wraight CA, Clayton RK (1973) The absolute quantum efficiency of bacteriochlorophyll photoxidation in reaction centers. Biochim Biophys Acta 333:246-260
    • (1973) Biochim Biophys Acta , vol.333 , pp. 246-260
    • Wraight, C.A.1    Clayton, R.K.2
  • 76
    • 77955802973 scopus 로고    scopus 로고
    • The acceptor quinones of purple photosynthetic bacteria - Structure and spectroscopy
    • N.C. Hunter F. Daldal M.C. Thurnauer J.T. Beatty (eds) Springer Dordrecht 10.1007/978-1-4020-8815-5-20
    • Wraight C, Gunner MR (2009) The acceptor quinones of purple photosynthetic bacteria - structure and spectroscopy. In: Hunter NC, Daldal F, Thurnauer MC, Beatty JT (eds) The purple phototropic bacteria. Springer, Dordrecht, pp 379-405
    • (2009) The Purple Phototropic Bacteria , pp. 379-405
    • Wraight, C.1    Gunner, M.R.2
  • 77
    • 0018898814 scopus 로고
    • Redox equilibrium in the acceptor quinone complex of isolated reaction centers and the mode of action of o-phenanthroline
    • 1:CAS:528:DyaL3cXitFajt78%3D 6966586 10.1016/0014-5793(80)80498-4
    • Wraight CA, Stein RR (1980) Redox equilibrium in the acceptor quinone complex of isolated reaction centers and the mode of action of o-phenanthroline. FEBS Lett 113:73-77
    • (1980) FEBS Lett , vol.113 , pp. 73-77
    • Wraight, C.A.1    Stein, R.R.2
  • 78
    • 0002269166 scopus 로고
    • Bacterial reaction centers as a model for photosystem II: Turn over of the secondary acceptor quinone
    • Y. Inoue A.R. Crofts Govindjee N. Murata G. Renger K. Satoh (eds) Academic Press New York
    • Wraight CA, Stein RR (1983) Bacterial reaction centers as a model for photosystem II: turn over of the secondary acceptor quinone. In: Inoue Y, Crofts AR, Govindjee, Murata N, Renger G, Satoh K (eds) The oxygen evolving system of photosynthesis. Academic Press, New York, pp 383-393
    • (1983) The Oxygen Evolving System of Photosynthesis , pp. 383-393
    • Wraight, C.A.1    Stein, R.R.2
  • 79
    • 50949087723 scopus 로고    scopus 로고
    • The 2-methoxy group of ubiquinone is essential for function of the acceptor quinones in reaction centers from Rba. Sphaeroides
    • 1:CAS:528:DC%2BD1cXnsFCmsro%3D 18474215 10.1016/j.bbabio.2008.04.025
    • Wraight CA, Vakkasoglu AS, Poluektov Y, Mattis AJ, Nihan D, Lipshutz BH (2008) The 2-methoxy group of ubiquinone is essential for function of the acceptor quinones in reaction centers from Rba. sphaeroides. Biochim Biophys Acta 1777:631-636
    • (2008) Biochim Biophys Acta , vol.1777 , pp. 631-636
    • Wraight, C.A.1    Vakkasoglu, A.S.2    Poluektov, Y.3    Mattis, A.J.4    Nihan, D.5    Lipshutz, B.H.6
  • 80
    • 0034710423 scopus 로고    scopus 로고
    • - Charge recombination in photosynthetic reaction centers
    • 1:CAS:528:DC%2BD3cXkvFamtbw%3D 10.1021/jp000543v
    • - charge recombination in photosynthetic reaction centers. J Phys Chem B 104:8035-8043
    • (2000) J Phys Chem B , vol.104 , pp. 8035-8043
    • Xu, Q.1    Gunner, M.R.2
  • 81
    • 0037176849 scopus 로고    scopus 로고
    • B electron transfer reaction in bacterial photosynthetic reaction centers: PH dependence of the conformational gating step
    • 1:CAS:528:DC%2BD38Xpt1SlsA%3D%3D 11851416 10.1021/bi011834c
    • B electron transfer reaction in bacterial photosynthetic reaction centers: pH dependence of the conformational gating step. Biochemistry 41:2694-2701
    • (2002) Biochemistry , vol.41 , pp. 2694-2701
    • Xu, Q.1    Gunner, M.R.2
  • 82
    • 11844302809 scopus 로고    scopus 로고
    • Energetics of quinone-dependent electron and proton transfers in Rhodobacter sphaeroides photosynthetic reaction centers
    • 1:CAS:528:DC%2BD2cXhtVCrsb3P 15628848 10.1021/bi048348k
    • Zhu Z, Gunner MR (2005) Energetics of quinone-dependent electron and proton transfers in Rhodobacter sphaeroides photosynthetic reaction centers. Biochemistry 44:82-96
    • (2005) Biochemistry , vol.44 , pp. 82-96
    • Zhu, Z.1    Gunner, M.R.2


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