메뉴 건너뛰기




Volumn , Issue , 2008, Pages 1-37

Bioenergetics and Biological Electron Transport

Author keywords

Bioenergetics and biological electron transport; Biological cells eukaryotic and prokaryotic; Chemiosmosis; Energetics redox potentials; Flavin adenine dinucleotide (FAD); Franck Condon principle; Iron sulfur clusters; NADH CoQ reductase complex

Indexed keywords


EID: 84889620993     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9780470753842.ch1     Document Type: Chapter
Times cited : (9)

References (132)
  • 1
    • 0003748396 scopus 로고
    • Integrated Chemical Systems
    • A Chemical Approach to Nanotechnology. John Wiley, New York
    • A. J. Bard, Integrated Chemical Systems. A Chemical Approach to Nanotechnology. John Wiley, New York, 1994.
    • (1994)
    • Bard, A.J.1
  • 3
    • 36949083936 scopus 로고
    • Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism
    • P. Mitchell, Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism, Nature, 191, 144-148 (1961).
    • (1961) Nature , vol.191 , pp. 144-148
    • Mitchell, P.1
  • 4
    • 0018784261 scopus 로고
    • Keilin's respiratory chain concept and its chemiosmotic consequences
    • P. Mitchell, Keilin's respiratory chain concept and its chemiosmotic consequences, Science, 206, 1148-1159 (1979).
    • (1979) Science , vol.206 , pp. 1148-1159
    • Mitchell, P.1
  • 5
    • 0036496185 scopus 로고    scopus 로고
    • Mechanism of the F1F0-type ATP synthase, a biological rotary motor
    • R. A. Capaldi, R. and Aggeler, Mechanism of the F1F0-type ATP synthase, a biological rotary motor, Trends Biochem. Sci., 27, 154-160 (2002).
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 154-160
    • Capaldi, R.A.1    Aggeler, R.2
  • 6
    • 0004279464 scopus 로고    scopus 로고
    • Molecular Mechanisms of Photosynthesis
    • Blackwell Science, Oxford
    • R. E. Blankenship, Molecular Mechanisms of Photosynthesis. Blackwell Science, Oxford, 2002.
    • (2002)
    • Blankenship, R.E.1
  • 7
    • 0033525773 scopus 로고    scopus 로고
    • Mitochondrial diseases in man and mouse
    • D. C. Wallace, Mitochondrial diseases in man and mouse, Science, 283, 1482-1488 (1999).
    • (1999) Science , vol.283 , pp. 1482-1488
    • Wallace, D.C.1
  • 8
    • 0037421839 scopus 로고    scopus 로고
    • The cost of living
    • P. Rich, The cost of living, Nature, 421, 583 (2003).
    • (2003) Nature , vol.421 , pp. 583
    • Rich, P.1
  • 9
    • 0034235229 scopus 로고    scopus 로고
    • The internal structure of mitochondria
    • T. G. Frey and C. A. Mannella, The internal structure of mitochondria, Trends Biochem. Sci., 25, 319-324 (2000).
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 319-324
    • Frey, T.G.1    Mannella, C.A.2
  • 10
    • 0033525924 scopus 로고    scopus 로고
    • Oxidative phosphorylation at the fin de siécle
    • M. Saraste, Oxidative phosphorylation at the fin de siécle, Science, 283, 1488-1493 (1999).
    • (1999) Science , vol.283 , pp. 1488-1493
    • Saraste, M.1
  • 11
    • 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, Ann. Rev. Biophys. Biomol. Struct., 30, 25-65 (2001).
    • (2001) Ann. Rev. Biophys. Biomol. Struct. , vol.30 , pp. 25-65
    • Schultz, B.E.1    Chan, S.I.2
  • 12
    • 0031592480 scopus 로고    scopus 로고
    • Three-dimensional structure of NADH-dehydrogenase from Neurospora crassa by electron microscopy and conical tilt reconstruction
    • V. Guénebaut, R. Vincentelli, D. Mills, H. Weiss and K. Leonard, Three-dimensional structure of NADH-dehydrogenase from Neurospora crassa by electron microscopy and conical tilt reconstruction, J. Mol. Biol., 265, 409-418 (1997).
    • (1997) J. Mol. Biol. , vol.265 , pp. 409-418
    • Guénebaut, V.1    Vincentelli, R.2    Mills, D.3    Weiss, H.4    Leonard, K.5
  • 13
    • 0033179604 scopus 로고    scopus 로고
    • Structure of the respiratory NADH:ubiquinone oxidoreductase (complex I)
    • N. Grigorieff, Structure of the respiratory NADH:ubiquinone oxidoreductase (complex I), Curr. Op. Struct. Biol., 9, 476-483 (1999).
    • (1999) Curr. Op. Struct. Biol. , vol.9 , pp. 476-483
    • Grigorieff, N.1
  • 14
    • 0026077298 scopus 로고
    • Electron microscopic analysis of peripheral and membrane parts of mitochondrial NADH dehydrogenase (complex I)
    • G. Hofhaus, H. Weiss and K. Leonard, Electron microscopic analysis of peripheral and membrane parts of mitochondrial NADH dehydrogenase (complex I), J. Mol. Biol., 221, 1027-1043 (1991).
    • (1991) J. Mol. Biol. , vol.221 , pp. 1027-1043
    • Hofhaus, G.1    Weiss, H.2    Leonard, K.3
  • 16
    • 23044477952 scopus 로고    scopus 로고
    • Organization of iron-sulfur clusters in respiratory complex I
    • P. Hinchliffe and L. A. Sazanov, Organization of iron-sulfur clusters in respiratory complex I, Science, 309, 771-774 (2005).
    • (2005) Science , vol.309 , pp. 771-774
    • Hinchliffe, P.1    Sazanov, L.A.2
  • 17
    • 33644872938 scopus 로고    scopus 로고
    • Structure of the hydrophilic domain of respiratory Complex I from Thermus thermophilus
    • L. A. Sazanova and P. Hinchliffe, Structure of the hydrophilic domain of respiratory Complex I from Thermus thermophilus, Science, 311, 1430-1436 (2006).
    • (2006) Science , vol.311 , pp. 1430-1436
    • Sazanova, L.A.1    Hinchliffe, P.2
  • 18
    • 0027481581 scopus 로고
    • The bacterial energy-transducing NADH-quinone oxidoreductase
    • T. Yagi, The bacterial energy-transducing NADH-quinone oxidoreductase, Biochim. Biophys. Acta, 1141, 1-17 (1993).
    • (1993) Biochim. Biophys. Acta , vol.1141 , pp. 1-17
    • Yagi, T.1
  • 19
    • 0025760073 scopus 로고
    • The respiratorychain NADH dehydrogenase (complex I) of mitochondria
    • H. Weiss, T. Friedrich, H. G. and D. Price, The respiratorychain NADH dehydrogenase (complex I) of mitochondria, Eur. J. Biochem., 197, 563-576 (1991).
    • (1991) Eur. J. Biochem. , vol.197 , pp. 563-576
    • Weiss, H.1    Friedrich, T.H.G.2    Price, D.3
  • 20
    • 0027290826 scopus 로고
    • NADH-quinone oxidoreductase, the most complex complex
    • T. Ohnishi, NADH-quinone oxidoreductase, the most complex complex, J. Bioenerg. Biomembr., 25, 325-329 (1993).
    • (1993) J. Bioenerg. Biomembr. , vol.25 , pp. 325-329
    • Ohnishi, T.1
  • 21
    • 0031033436 scopus 로고    scopus 로고
    • Proton-translocation by membrane-bound NADH: ubiquinone-oxidoreductase (complex I) through redox-gated ligand conduction
    • U. Brandt, Proton-translocation by membrane-bound NADH: ubiquinone-oxidoreductase (complex I) through redox-gated ligand conduction, Biochim. Biophys. Acta, 1318, 79-81 (1997).
    • (1997) Biochim. Biophys. Acta , vol.1318 , pp. 79-81
    • Brandt, U.1
  • 22
    • 0010049951 scopus 로고    scopus 로고
    • Structure of fumarate reductase from Wolinella succinogenes at 2.2 Å resolution
    • C. R. D. Lancaster, A. Kröger, M. Auer and H. Michel, Structure of fumarate reductase from Wolinella succinogenes at 2.2 Å resolution, Nature, 402, 377-385 (1999).
    • (1999) Nature , vol.402 , pp. 377-385
    • Lancaster, C.R.D.1    Kröger, A.2    Auer, M.3    Michel, H.4
  • 23
    • 0030600143 scopus 로고    scopus 로고
    • A structural model for the membrane-integral domain of succinate:quinone oxidoreductase
    • C. Hägerhäll and L. Hederstedt, A structural model for the membrane-integral domain of succinate:quinone oxidoreductase, FEBS Lett., 389, 25-31 (1996).
    • (1996) FEBS Lett. , vol.389 , pp. 25-31
    • Hägerhäll, C.1    Hederstedt, L.2
  • 24
    • 0343052744 scopus 로고    scopus 로고
    • Succinate: quinone oxidoreductases. Variations on a conserved theme
    • C. Hägerhäll, Succinate: quinone oxidoreductases. Variations on a conserved theme, Biochim. Biophys. Acta, 1320, 107-141 (1997).
    • (1997) Biochim. Biophys. Acta , vol.1320 , pp. 107-141
    • Hägerhäll, C.1
  • 25
    • 0033580880 scopus 로고    scopus 로고
    • Structure of the Escherichia coli fumerate reductase respiratory complex
    • T. M. Iverson, C. Luna-Chavez, G. Cecchini and D. C. Rees, Structure of the Escherichia coli fumerate reductase respiratory complex, Science, 284, 1961 (1999).
    • (1999) Science , vol.284 , pp. 1961
    • Iverson, T.M.1    Luna-Chavez, C.2    Cecchini, G.3    Rees, D.C.4
  • 26
    • 0025358947 scopus 로고
    • The protonmotive Q cycle
    • B. L. Trumpower, The protonmotive Q cycle, J. Biol. Chem., 265, 11409-11412 (1990).
    • (1990) J. Biol. Chem. , vol.265 , pp. 11409-11412
    • Trumpower, B.L.1
  • 27
    • 0035399478 scopus 로고    scopus 로고
    • Large scale domain movement in cytochrome bc1: a new device for electron transfer in proteins
    • E. Darrouzet, C. C. Moser, P. L. Dutton and F. Daldal, Large scale domain movement in cytochrome bc1: a new device for electron transfer in proteins, Trends Biochem. Sci., 26, 445-451 (2001).
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 445-451
    • Darrouzet, E.1    Moser, C.C.2    Dutton, P.L.3    Daldal, F.4
  • 29
    • 1342325555 scopus 로고    scopus 로고
    • Reversible redox energy coupling in electron transfer chains
    • A. Osyczka, C. C. Moser, F. Daidal and P. L. Dutton, Reversible redox energy coupling in electron transfer chains, Nature, 427, 607-612 (2004).
    • (2004) Nature , vol.427 , pp. 607-612
    • Osyczka, A.1    Moser, C.C.2    Daidal, F.3    Dutton, P.L.4
  • 32
    • 0025640889 scopus 로고
    • Structural features of cytochrome-oxidase
    • M. Saraste, Structural features of cytochrome-oxidase, Quart. Rev. Biophys., 23, 331-366 (1990).
    • (1990) Quart. Rev. Biophys. , vol.23 , pp. 331-366
    • Saraste, M.1
  • 33
    • 0028137093 scopus 로고
    • The cytochrome oxidase superfamily of redox-driven proton pumps
    • M. W. Calhoun, J. W. Thomas and R. B. Gennis, The cytochrome oxidase superfamily of redox-driven proton pumps, Trends Biochem. Sci., 19, 325-330 (1994).
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 325-330
    • Calhoun, M.W.1    Thomas, J.W.2    Gennis, R.B.3
  • 34
    • 0026530174 scopus 로고
    • Oxygen activation and the conservation of energy in cell respiration
    • G. T. Babcock and M. Wilksẗom, Oxygen activation and the conservation of energy in cell respiration, Nature, 356, 301-309 (1992).
    • (1992) Nature , vol.356 , pp. 301-309
    • Babcock, G.T.1    Wilksẗom, M.2
  • 36
    • 0034640504 scopus 로고    scopus 로고
    • Proton pumping by cytochome oxidase: progress, problems and postulates
    • D. Zaslavsky and R. B. Gennis, Proton pumping by cytochome oxidase: progress, problems and postulates, Biochim. Biophys. Acta, 1458, 164-179 (2000).
    • (2000) Biochim. Biophys. Acta , vol.1458 , pp. 164-179
    • Zaslavsky, D.1    Gennis, R.B.2
  • 37
    • 0029150334 scopus 로고
    • Purpose of proton pathways
    • R. J. P. Williams, Purpose of proton pathways, Nature, 376, 643 (1995).
    • (1995) Nature , vol.376 , pp. 643
    • Williams, R.J.P.1
  • 39
    • 0028890031 scopus 로고
    • Structure at 2.8A ° resolution of cytochrome c oxidase from Paracoccus denitrificans
    • S. Iwata, C. Ostermeier, B. Ludwig and H. Michel, Structure at 2.8A ° resolution of cytochrome c oxidase from Paracoccus denitrificans, Nature, 376, 660-669 (1995).
    • (1995) Nature , vol.376 , pp. 660-669
    • Iwata, S.1    Ostermeier, C.2    Ludwig, B.3    Michel, H.4
  • 40
    • 24644471025 scopus 로고    scopus 로고
    • A mechanistic principle for proton pumping by cytochrome c oxidase
    • K. Faxén, G. Gilderson, P. Adelroth and P. Brzezinski, A mechanistic principle for proton pumping by cytochrome c oxidase, Nature, 437, 286-289 (2005).
    • (2005) Nature , vol.437 , pp. 286-289
    • Faxén, K.1    Gilderson, G.2    Adelroth, P.3    Brzezinski, P.4
  • 41
    • 0038998833 scopus 로고    scopus 로고
    • Proton translocation by cytochrome c oxidase: a rejoinder to recent criticism
    • M.Wikström, Proton translocation by cytochrome c oxidase: a rejoinder to recent criticism, Biochem., 39, 3515-3519 (2000).
    • (2000) Biochem. , vol.39 , pp. 3515-3519
    • Wikström, M.1
  • 42
    • 0023887173 scopus 로고
    • Bacterial electron transport chains
    • Y. Anraku, Bacterial electron transport chains, Ann. Rev. Biochem., 57, 101-132 (1988).
    • (1988) Ann. Rev. Biochem. , vol.57 , pp. 101-132
    • Anraku, Y.1
  • 43
    • 84889623411 scopus 로고    scopus 로고
    • Energy transduction processes: from respiration to photosynthesis in The Desk Encyclopedia of Microbiology
    • M. Schaechter (ed.), Elsevier
    • S. J. Ferguson, Energy transduction processes: from respiration to photosynthesis in The Desk Encyclopedia of Microbiology, M. Schaechter (ed.), Elsevier, 2003, pp. 392-400.
    • (2003) , pp. 392-400
    • Ferguson, S.J.1
  • 44
    • 0033525788 scopus 로고    scopus 로고
    • Mitochondrial evolution
    • M. W. Gray, G. Burger and B. F. Lang, Mitochondrial evolution, Science, 283, 1476-1481 (1999).
    • (1999) Science , vol.283 , pp. 1476-1481
    • Gray, M.W.1    Burger, G.2    Lang, B.F.3
  • 45
    • 0027219326 scopus 로고
    • Na{thorn}-translocating NADHquinone reductase of marine and halophilic bacteria
    • T. Unemoto and M. Hayashi, Na{thorn}-translocating NADHquinone reductase of marine and halophilic bacteria, J. Mol. Biol., 25, 385-391 (1993).
    • (1993) J. Mol. Biol. , vol.25 , pp. 385-391
    • Unemoto, T.1    Hayashi, M.2
  • 47
    • 0034662927 scopus 로고    scopus 로고
    • The crystal structure of D-lactate dehydrogenase, a peripheral membrane respiratory enzyme
    • O. Dym, E. A. Pratt, C. Ho and D. Eisenberg, The crystal structure of D-lactate dehydrogenase, a peripheral membrane respiratory enzyme, Biochem., 97, 9413-9418 (2000).
    • (2000) Biochem. , vol.97 , pp. 9413-9418
    • Dym, O.1    Pratt, E.A.2    Ho, C.3    Eisenberg, D.4
  • 48
    • 84889614723 scopus 로고    scopus 로고
    • Electron transport and energy transduction in Photosynthesis: A Comprehensive Treatise
    • A. S. Raghavendra (ed.), Cambridge University Press, Cambridge, Chapter 7
    • J. Whitmarsh, Electron transport and energy transduction in Photosynthesis: A Comprehensive Treatise, A. S. Raghavendra (ed.), Cambridge University Press, Cambridge, 1997, Chapter 7.
    • (1997)
    • Whitmarsh, J.1
  • 49
    • 0037047319 scopus 로고    scopus 로고
    • Photosynthesis of ATP-electrons, proton pumps, rotors, and poise
    • J. F. Allen, Photosynthesis of ATP-electrons, proton pumps, rotors, and poise, Cell, 110, 273-276 (2002).
    • (2002) Cell , vol.110 , pp. 273-276
    • Allen, J.F.1
  • 50
    • 0034952381 scopus 로고    scopus 로고
    • The structure of photosystem I
    • J. Barber, The structure of photosystem I, Nature Struct. Biol., 8, 577-579 (2001).
    • (2001) Nature Struct. Biol. , vol.8 , pp. 577-579
    • Barber, J.1
  • 51
    • 11044234285 scopus 로고    scopus 로고
    • Supramolecular organization of thylakoid membrane proteins in green plants
    • J. P. Dekker and E. J. Boekema, Supramolecular organization of thylakoid membrane proteins in green plants, Biochim, Biophys. Acta, 1706, 12-39 (2005).
    • (2005) Biochim, Biophys. Acta , vol.1706 , pp. 12-39
    • Dekker, J.P.1    Boekema, E.J.2
  • 54
    • 1642602038 scopus 로고    scopus 로고
    • Crystal structure of spinach major lightharvesting complex at 2.72 A ° resolution
    • Z. Liu, H. Yan, K. Wang, T. Kuang, J. Zhang, L. Gui, X. An and W. Chang, Crystal structure of spinach major lightharvesting complex at 2.72 A ° resolution, Nature, 428, 287-292 (2004).
    • (2004) Nature , vol.428 , pp. 287-292
    • Liu, Z.1    Yan, H.2    Wang, K.3    Kuang, T.4    Zhang, J.5    Gui, L.6    An, X.7    Chang, W.8
  • 55
    • 30744445692 scopus 로고    scopus 로고
    • Towards complete cofactor arrangement in the 3.0 A ° resolution structure of photosystem II
    • B. Loll, J. Kern, W. Saenger, A. Zouni and J. Biesiadka, Towards complete cofactor arrangement in the 3.0 A ° resolution structure of photosystem II, Nature, 438, 1040-1043 (2005).
    • (2005) Nature , vol.438 , pp. 1040-1043
    • Loll, B.1    Kern, J.2    Saenger, W.3    Zouni, A.4    Biesiadka, J.5
  • 57
    • 0035825682 scopus 로고    scopus 로고
    • Crystal structure of photosystem II from Synechococcus elongatus at 3.8 Å resolution
    • A. Zouni, H.-T. Witt, J. Kern, P. Fromme, N. Krauß, W. Saenger and P. Orth, Crystal structure of photosystem II from Synechococcus elongatus at 3.8 Å resolution, Nature, 409, 739-743 (2001).
    • (2001) Nature , vol.409 , pp. 739-743
    • Zouni, A.1    Witt, H.-T.2    Kern, J.3    Fromme, P.4    Krauß, N.5    Saenger, W.6    Orth, P.7
  • 58
    • 0036469776 scopus 로고    scopus 로고
    • Reaction centres: the structure and evolution of biological solar power
    • P. Heathcote, P. K. Fyfe and M. R. Jones, Reaction centres: the structure and evolution of biological solar power, Trends Biochem. Sci., 27, 79-87 (2002).
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 79-87
    • Heathcote, P.1    Fyfe, P.K.2    Jones, M.R.3
  • 59
    • 1642331709 scopus 로고    scopus 로고
    • Architecture of the photosynthetic oxygen-evolving center
    • K. N. Ferreira, T. M. Iverson, K. Maghlaoui, J. Barber and S. Iwata, Architecture of the photosynthetic oxygen-evolving center, Science, 303, 1831-1838 (2004).
    • (2004) Science , vol.303 , pp. 1831-1838
    • Ferreira, K.N.1    Iverson, T.M.2    Maghlaoui, K.3    Barber, J.4    Iwata, S.5
  • 60
    • 0037422557 scopus 로고    scopus 로고
    • Crystal structure of oxygenevolving photosystem II from Thermosynechococcus vulcanus at 3.7 A resolution
    • N. Kamiya and J.-R. Shen, Crystal structure of oxygenevolving photosystem II from Thermosynechococcus vulcanus at 3.7 A resolution, Proc. Nat. Acad. Sci., 100, 98-103 (2003).
    • (2003) Proc. Nat. Acad. Sci. , vol.100 , pp. 98-103
    • Kamiya, N.1    Shen, J.-R.2
  • 61
    • 0142231010 scopus 로고    scopus 로고
    • Mechanisms for photosystems I and II
    • N. Krauß, Mechanisms for photosystems I and II, Curr. Op. Chem. Biol., 7, 540-550 (2003).
    • (2003) Curr. Op. Chem. Biol. , vol.7 , pp. 540-550
    • Krauß, N.1
  • 62
    • 0030854151 scopus 로고    scopus 로고
    • A metalloradical mechanism for the generation of oxygen from water photosynthesis
    • C. W. Hoganson, A metalloradical mechanism for the generation of oxygen from water photosynthesis, Science, 277, 1953-1956 (1997).
    • (1997) Science , vol.277 , pp. 1953-1956
    • Hoganson, C.W.1
  • 63
    • 0242494128 scopus 로고    scopus 로고
    • Structure of the cytochrome b6 f complex of oxygenic photosynthesis: tuning the cavity
    • G. Kurisu, H. Zhang, J. L. Smith andW. A. Cramer, Structure of the cytochrome b6 f complex of oxygenic photosynthesis: tuning the cavity, Science, 302, 1009-1014 (2003).
    • (2003) Science , vol.302 , pp. 1009-1014
    • Kurisu, G.1    Zhang, H.2    Smith, J.L.3    Cramer, W.A.4
  • 64
    • 0035927420 scopus 로고    scopus 로고
    • Three-dimensional structure of cyanobacterial photosystem I at 2.5 A ° resolution
    • P. Jordan, P. Fromme, H.-T.Witt, O. Klukas,W. Saenger and N. Krauß, Three-dimensional structure of cyanobacterial photosystem I at 2.5 A ° resolution, Nature, 411, 909-917 (2001).
    • (2001) Nature , vol.411 , pp. 909-917
    • Jordan, P.1    Fromme, P.2    Witt, H.-T.3    Klukas, O.4    Saenger, W.5    Krauß, N.6
  • 65
    • 0035927660 scopus 로고    scopus 로고
    • Chlorophylls galore
    • W. Kühlbrandt, Chlorophylls galore, Nature, 411, 896-897 (2001).
    • (2001) Nature , vol.411 , pp. 896-897
    • Kühlbrandt, W.1
  • 66
    • 0028921929 scopus 로고
    • Refined crystal structure of spinach ferredoxin reductase at 1.7 A ° resolution: oxidized, reduced and 20-phospho-S0-AMP bound states
    • C. M. Bruns and P. A. Karplus, Refined crystal structure of spinach ferredoxin reductase at 1.7 A ° resolution: oxidized, reduced and 20-phospho-S0-AMP bound states, J. Mol. Biol., 247, 124-145 (1995).
    • (1995) J. Mol. Biol. , vol.247 , pp. 124-145
    • Bruns, C.M.1    Karplus, P.A.2
  • 67
    • 0348148910 scopus 로고    scopus 로고
    • Crystal structure of plant photsystem I
    • A. Ben-Shem, F. Frolow and N. Nelson, Crystal structure of plant photsystem I, Nature, 426, 630-635 (2003).
    • (2003) Nature , vol.426 , pp. 630-635
    • Ben-Shem, A.1    Frolow, F.2    Nelson, N.3
  • 68
    • 0024433591 scopus 로고
    • The photosynthetic reaction center from purple bacterium Rhodopseudomonas viridis
    • J. Deisenhofer and H. Michel, The photosynthetic reaction center from purple bacterium Rhodopseudomonas viridis, Science, 245, 1463-1473 (1989).
    • (1989) Science , vol.245 , pp. 1463-1473
    • Deisenhofer, J.1    Michel, H.2
  • 69
    • 0015992799 scopus 로고
    • Redox potentials of certain vitamins K: implications for a role in sulfite reduction by obligately anaerobic bacteria
    • G. C. Wagner, R. J. Kassner and M. D. Kamen, Redox potentials of certain vitamins K: implications for a role in sulfite reduction by obligately anaerobic bacteria, Proc. Nat. Acad. Sci., 71, 253-256 (1974).
    • (1974) Proc. Nat. Acad. Sci. , vol.71 , pp. 253-256
    • Wagner, G.C.1    Kassner, R.J.2    Kamen, M.D.3
  • 71
    • 0001209090 scopus 로고
    • Flavin coenzymes: at the crossroads of biological redox chemistry
    • C. Walsh, Flavin coenzymes: at the crossroads of biological redox chemistry, Acc. Chem. Res., 13, 148-155 (1980).
    • (1980) Acc. Chem. Res. , vol.13 , pp. 148-155
    • Walsh, C.1
  • 72
    • 0030868605 scopus 로고    scopus 로고
    • Iron-sulfur clusters: nature's modular, multipurpose structures
    • H. Beinert, R. H. Holm and E. Münck, Iron-sulfur clusters: nature's modular, multipurpose structures, Science, 277, 652-659 (1997).
    • (1997) Science , vol.277 , pp. 652-659
    • Beinert, H.1    Holm, R.H.2    Münck, E.3
  • 73
    • 0004236008 scopus 로고
    • The Biological Chemistry of the Elements
    • Oxford University Press, Oxford
    • J. J. R. Fraústo da Silva and R. J. P.Williams, The Biological Chemistry of the Elements, Oxford University Press, Oxford, 1993.
    • (1993)
    • Fraústo Da Silva, J.J.R.1    Williams, R.J.P.2
  • 74
    • 0032974116 scopus 로고    scopus 로고
    • Mechanisms for regulating electron transfer in multi-centre redox proteins
    • R. E. Sharp and S. K. Chapman, Mechanisms for regulating electron transfer in multi-centre redox proteins, Biochim. Biophys. Acta, 1432, 143-158 (1999).
    • (1999) Biochim. Biophys. Acta , vol.1432 , pp. 143-158
    • Sharp, R.E.1    Chapman, S.K.2
  • 75
    • 0015473745 scopus 로고
    • Membrane proteins
    • G. Guidotti, Membrane proteins, Ann. Rev. Biochem., 41, 731-752 (1972).
    • (1972) Ann. Rev. Biochem. , vol.41 , pp. 731-752
    • Guidotti, G.1
  • 76
    • 0015784154 scopus 로고
    • Lipid composition of plant mitochondria and of chloroplasts
    • H. A. Schwertner and J. B. Biale, Lipid composition of plant mitochondria and of chloroplasts, J. Lipid Res., 14, 235-242 (1973).
    • (1973) J. Lipid Res. , vol.14 , pp. 235-242
    • Schwertner, H.A.1    Biale, J.B.2
  • 77
    • 22144463880 scopus 로고    scopus 로고
    • Metabolism and functions of phosphatidylserine
    • J. E. Vance and R. Steenbergen, Metabolism and functions of phosphatidylserine, Prog. Lipid Res., 44, 207-234 (2005).
    • (2005) Prog. Lipid Res. , vol.44 , pp. 207-234
    • Vance, J.E.1    Steenbergen, R.2
  • 78
    • 84889622373 scopus 로고    scopus 로고
    • Composition and role of phospholipids in the body
    • in Encyclopedia of Human Nutrition, B. Caballero, L. Allen and A. Prentice (eds.), Elsevier Science, London
    • A. D. Postle, Composition and role of phospholipids in the body, in Encyclopedia of Human Nutrition, B. Caballero, L. Allen and A. Prentice (eds.), Elsevier Science, London, 2005, pp 132-142.
    • (2005) , pp. 132-142
    • Postle, A.D.1
  • 79
    • 0030996718 scopus 로고    scopus 로고
    • Control of metalloprotein redox potentials: what does site-directed mutagenesis of hemoproteins tell us?
    • A. G. Mauk and G. R. Moore, Control of metalloprotein redox potentials: what does site-directed mutagenesis of hemoproteins tell us? J. Bio. Inorg. Chem., 2, 119-125 (1997).
    • (1997) J. Bio. Inorg. Chem , vol.2 , pp. 119-125
    • Mauk, A.G.1    Moore, G.R.2
  • 80
    • 0035215509 scopus 로고    scopus 로고
    • Medium and temperature effects on the redox chemistry of cytochrome c
    • G. Battistuzzi, M. Borsari and M. Sola, Medium and temperature effects on the redox chemistry of cytochrome c, Eur. J. Inorg. Chem., 12, 2989-3004 (2001).
    • (2001) Eur. J. Inorg. Chem. , vol.12 , pp. 2989-3004
    • Battistuzzi, G.1    Borsari, M.2    Sola, M.3
  • 81
    • 0024495355 scopus 로고
    • Effects of buried ionizable amino acids on the reduction potential of recombinant myoglobin
    • R. Varadarajan, T. E. Zewert, H. B. Gray and S. G. Boxer, Effects of buried ionizable amino acids on the reduction potential of recombinant myoglobin, Science, 243, 69-72 (1989).
    • (1989) Science , vol.243 , pp. 69-72
    • Varadarajan, R.1    Zewert, T.E.2    Gray, H.B.3    Boxer, S.G.4
  • 82
    • 0037006983 scopus 로고    scopus 로고
    • A multigeneration analysis of cytochrome b562 redox variants: evolutionary strategies for modulating redox potential revealed using a library approach
    • S. L. Springs, S. E. Bass, G. Bowman, I. Nodelman, C. E. Schutt and G. L. McLendon, A multigeneration analysis of cytochrome b562 redox variants: evolutionary strategies for modulating redox potential revealed using a library approach, Biochem., 41, 4321-4328 (2002).
    • (2002) Biochem. , vol.41 , pp. 4321-4328
    • Springs, S.L.1    Bass, S.E.2    Bowman, G.3    Nodelman, I.4    Schutt, C.E.5    McLendon, G.L.6
  • 83
    • 0027955916 scopus 로고
    • Site-directed mutagenesis of tyrosine-98 in the flavodoxin from Desulfovibrio vulgaris (Hildenborough): regulation of oxidation-reduction properties of the bound FMN cofactor by aromatic, solvent, and electrostatic interactions
    • R. P. Swenson and G. D. Krey, Site-directed mutagenesis of tyrosine-98 in the flavodoxin from Desulfovibrio vulgaris (Hildenborough): regulation of oxidation-reduction properties of the bound FMN cofactor by aromatic, solvent, and electrostatic interactions, Biochem., 33, 8505-8514 (1994).
    • (1994) Biochem. , vol.33 , pp. 8505-8514
    • Swenson, R.P.1    Krey, G.D.2
  • 84
    • 0028946646 scopus 로고
    • Electrostatic effects of surface acidic amino acid residues on the oxidation-reduction potentials of the flavodoxin from Desulfovibrio vulgaris (Hildenborough)
    • Z. Zhou and R. P. Swenson, Electrostatic effects of surface acidic amino acid residues on the oxidation-reduction potentials of the flavodoxin from Desulfovibrio vulgaris (Hildenborough), Biochem., 34, 3183-3192 (1995).
    • (1995) Biochem. , vol.34 , pp. 3183-3192
    • Zhou, Z.1    Swenson, R.P.2
  • 85
    • 0030456586 scopus 로고    scopus 로고
    • The cumulative electrostatic effect of aromatic stacking interactions and the negative electrostatic environment if the flavin mononucleotide binding site is a major determinant of the reduction potential of the flavodoxin from Desulfovibrio vulgans (Hildenborough)
    • Z. Zhou and R. P. Swenson, The cumulative electrostatic effect of aromatic stacking interactions and the negative electrostatic environment if the flavin mononucleotide binding site is a major determinant of the reduction potential of the flavodoxin from Desulfovibrio vulgans (Hildenborough), Biochem., 35, 15980-15988 (1996).
    • (1996) Biochem. , vol.35 , pp. 15980-15988
    • Zhou, Z.1    Swenson, R.P.2
  • 86
    • 0032475447 scopus 로고    scopus 로고
    • Modulation of flavin recognition and redox properties through donor atom-p interactions
    • E. C. Breinlinger, C. J. Keenan and V. M. Rotello, Modulation of flavin recognition and redox properties through donor atom-p interactions, J. Am. Chem. Soc., 120, 8606-8609 (1998).
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 8606-8609
    • Breinlinger, E.C.1    Keenan, C.J.2    Rotello, V.M.3
  • 87
    • 0031035026 scopus 로고    scopus 로고
    • Model systems for flavoprotein activity. Modulation of flavin redox potentials through p-stacking interactions
    • E. C. Breinlinger and V. M. Rotello, Model systems for flavoprotein activity. Modulation of flavin redox potentials through p-stacking interactions, J. Am. Chem. Soc., 119, 1165-1166 (1997).
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 1165-1166
    • Breinlinger, E.C.1    Rotello, V.M.2
  • 89
    • 0003486442 scopus 로고    scopus 로고
    • Electron Transfer in Chemistry and Biology
    • An Introduction to the Theory, John Wiley & Sons Ltd., Chichester
    • A. M. Kuznetsov and J. Ulstrup, Electron Transfer in Chemistry and Biology. An Introduction to the Theory, John Wiley & Sons Ltd., Chichester 1999.
    • (1999)
    • Kuznetsov, A.M.1    Ulstrup, J.2
  • 90
    • 33748216903 scopus 로고
    • Electron transfer reactions in chemistry: theory and experiment
    • R. A. Marcus, Electron transfer reactions in chemistry: theory and experiment, Angew. Chem. Int. Ed. Engl., 32, 1111-1121 (1993).
    • (1993) Angew. Chem. Int. Ed. Engl. , vol.32 , pp. 1111-1121
    • Marcus, R.A.1
  • 91
    • 0022004980 scopus 로고
    • Electron transfers in chemistry and biology
    • R. A. Marcus and N. Sutin, Electron transfers in chemistry and biology, Biochim. Biophys. Acta, 811, 265-322 (1985).
    • (1985) Biochim. Biophys. Acta , vol.811 , pp. 265-322
    • Marcus, R.A.1    Sutin, N.2
  • 92
    • 0345330736 scopus 로고
    • Electron transfer in rutheniummodified proteins
    • J. R.Winkler and H. B. Gray, Electron transfer in rutheniummodified proteins, Chem. Rev., 92, 369-379 (1992).
    • (1992) Chem. Rev. , vol.92 , pp. 369-379
    • Winkler, J.R.1    Gray, H.B.2
  • 94
    • 1442328094 scopus 로고    scopus 로고
    • Electron tunneling through proteins
    • H. B. Gray and J. R. Winkler, Electron tunneling through proteins, Quart. Rev. Biophys., 36, 341-372 (2003).
    • (2003) Quart. Rev. Biophys. , vol.36 , pp. 341-372
    • Gray, H.B.1    Winkler, J.R.2
  • 96
    • 0038442872 scopus 로고    scopus 로고
    • Electron transport in molecular wire junctions
    • A. Nitzan and M. A. Ratner, Electron transport in molecular wire junctions, Science, 300, 1384-1389 (2003).
    • (2003) Science , vol.300 , pp. 1384-1389
    • Nitzan, A.1    Ratner, M.A.2
  • 97
    • 0007758337 scopus 로고
    • Peptide-mediated intramolecular electron transfer: long-range distance dependence
    • S. S. Isied, M. Y. Ogawa and J. F.Wishart, Peptide-mediated intramolecular electron transfer: long-range distance dependence, Chem. Rev., 92, 381-394 (1992).
    • (1992) Chem. Rev. , vol.92 , pp. 381-394
    • Isied, S.S.1    Ogawa, M.Y.2    Wishart, J.F.3
  • 98
    • 0026434593 scopus 로고
    • Protein electron transfer rates set by the bridging secondary and tertiary structure
    • D. N. Beratan, J. N. Betts and J. N. Onuchic, Protein electron transfer rates set by the bridging secondary and tertiary structure, Science, 252, 1285-1288 (1991).
    • (1991) Science , vol.252 , pp. 1285-1288
    • Beratan, D.N.1    Betts, J.N.2    Onuchic, J.N.3
  • 101
    • 14844360343 scopus 로고    scopus 로고
    • Long-range electron transfer
    • H. B. Gray and J. R. Winkler, Long-range electron transfer, Proc. Nat. Acad. Sci., 102, 3534-3539 (2005).
    • (2005) Proc. Nat. Acad. Sci. , vol.102 , pp. 3534-3539
    • Gray, H.B.1    Winkler, J.R.2
  • 103
    • 0033523919 scopus 로고    scopus 로고
    • Natural engineering principles of electron tunnelling in biological oxidation-reduction
    • C. C. Page, C. C. Moser, X. Chen and P. L. Dutton, Natural engineering principles of electron tunnelling in biological oxidation-reduction, Nature, 402, 47-52 (1999).
    • (1999) Nature , vol.402 , pp. 47-52
    • Page, C.C.1    Moser, C.C.2    Chen, X.3    Dutton, P.L.4
  • 104
    • 0142231009 scopus 로고    scopus 로고
    • Mechanism for electron transfer within and between proteins
    • C. C. Page, C. C. Moser and P. L. Dutton, Mechanism for electron transfer within and between proteins, Curr. Op. Chem. Biol., 7, 551-556 (2003).
    • (2003) Curr. Op. Chem. Biol. , vol.7 , pp. 551-556
    • Page, C.C.1    Moser, C.C.2    Dutton, P.L.3
  • 106
    • 0029895160 scopus 로고    scopus 로고
    • Electron transfer in proteins
    • H. B. Gray and J. R. Winkler, Electron transfer in proteins, Ann. Rev. Biochem., 65, 537-561 (1996).
    • (1996) Ann. Rev. Biochem. , vol.65 , pp. 537-561
    • Gray, H.B.1    Winkler, J.R.2
  • 107
    • 28144438785 scopus 로고    scopus 로고
    • The nature of aqueous tunneling pathways between electron-transfer proteins
    • J. Lin, I. A. Balabin and D. N. Beratan, The nature of aqueous tunneling pathways between electron-transfer proteins, Science, 310, 1311-1313 (2005).
    • (2005) Science , vol.310 , pp. 1311-1313
    • Lin, J.1    Balabin, I.A.2    Beratan, D.N.3
  • 108
    • 0027499733 scopus 로고
    • Soluble proteins: size, shape and function
    • D. S. Goodsell and A. L. Olson, Soluble proteins: size, shape and function, Trends Biochem. Sci., 18, 65-68 (1993).
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 65-68
    • Goodsell, D.S.1    Olson, A.L.2
  • 109
    • 48549111326 scopus 로고
    • Why are enzymes so big?
    • P. A. Srere, Why are enzymes so big? Trends Biochem. Sci., 9, 387-390 (1984).
    • (1984) Trends Biochem. Sci , vol.9 , pp. 387-390
    • Srere, P.A.1
  • 110
    • 49049126766 scopus 로고
    • Why are enzymes so large?
    • T. A. Payens, Why are enzymes so large? Trends Biochem. Sci., 8, 46 (1983).
    • (1983) Trends Biochem. Sci , vol.8 , pp. 46
    • Payens, T.A.1
  • 111
    • 0028314680 scopus 로고
    • Structure-function relations for ferredoxin reductase
    • P. A. Karplus and C. M. Bruns, Structure-function relations for ferredoxin reductase, J. Bioenerg. Biomembr., 26, 89-99 (1994).
    • (1994) J. Bioenerg. Biomembr. , vol.26 , pp. 89-99
    • Karplus, P.A.1    Bruns, C.M.2
  • 112
    • 0026023225 scopus 로고
    • Atomic structure of ferredoxin-NADP{thorn} reductase: prototype for a structurally novel flavoenzyme family
    • P. A. Karplus, M. J. Daniels and J. R. Herriott, Atomic structure of ferredoxin-NADP{thorn} reductase: prototype for a structurally novel flavoenzyme family, Science, 251, 60-66 (1991).
    • (1991) Science , vol.251 , pp. 60-66
    • Karplus, P.A.1    Daniels, M.J.2    Herriott, J.R.3
  • 113
    • 0024421234 scopus 로고
    • Substrate binding and catalysis by glutathione reductase as derived from refined enzyme: substrate crystal structures at 2 A ° resolution
    • P. A. Karplus and G. E. Schulz, Substrate binding and catalysis by glutathione reductase as derived from refined enzyme: substrate crystal structures at 2 A ° resolution, J. Mol. Biol., 210, 163-180 (1989).
    • (1989) J. Mol. Biol. , vol.210 , pp. 163-180
    • Karplus, P.A.1    Schulz, G.E.2
  • 114
    • 0024286097 scopus 로고
    • Crtystallographic analysis of the binding of NADPH, NADPH fragments, and NADPH analogues to glutathione reductase
    • E. F. Pai, P. A. Karplus and G. E. Schulz, Crtystallographic analysis of the binding of NADPH, NADPH fragments, and NADPH analogues to glutathione reductase, Biochem., 27, 4465-4474 (1988).
    • (1988) Biochem. , vol.27 , pp. 4465-4474
    • Pai, E.F.1    Karplus, P.A.2    Schulz, G.E.3
  • 115
    • 0032560652 scopus 로고    scopus 로고
    • Keeping up with the F1-ATPase
    • H. C. Berg, Keeping up with the F1-ATPase, Nature, 394, 324-325 (1998).
    • (1998) Nature , vol.394 , pp. 324-325
    • Berg, H.C.1
  • 116
    • 0031008228 scopus 로고    scopus 로고
    • The ATP synthase-a splendid molecular machine
    • P. D. Boyer, The ATP synthase-a splendid molecular machine, Ann. Rev. Biochem., 66, 717-749 (1997).
    • (1997) Ann. Rev. Biochem. , vol.66 , pp. 717-749
    • Boyer, P.D.1
  • 117
    • 0033581939 scopus 로고    scopus 로고
    • What makes ATP synthase spin?
    • P. D. Boyer, What makes ATP synthase spin? Nature, 402, 247-249 (1999).
    • (1999) Nature , vol.402 , pp. 247-249
    • Boyer, P.D.1
  • 120
    • 0030955244 scopus 로고    scopus 로고
    • Subunit rotation in Escherichia coli F0F1-ATPase synthase during oxidative phosphorylation
    • Y. Zhou, T. M. Duncan and R. L. Cross, Subunit rotation in Escherichia coli F0F1-ATPase synthase during oxidative phosphorylation, Proc. Natl. Acad. Sci., 94, 10583-10587 (1997).
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 10583-10587
    • Zhou, Y.1    Duncan, T.M.2    Cross, R.L.3
  • 121
    • 0029893335 scopus 로고    scopus 로고
    • Intersubunit rotation in active F-ATPase
    • D. Sabbert, S. Engelbrecht and W. Junge, Intersubunit rotation in active F-ATPase, Nature, 381, 623-625 (1996).
    • (1996) Nature , vol.381 , pp. 623-625
    • Sabbert, D.1    Engelbrecht, S.2    Junge, W.3
  • 122
    • 0033581879 scopus 로고    scopus 로고
    • Structural changes linked to proton translocation by subunit c of the ATP synthase
    • V. K. Rastogi and M. E. Girvin, Structural changes linked to proton translocation by subunit c of the ATP synthase, Nature, 402, 263-268 (1999).
    • (1999) Nature , vol.402 , pp. 263-268
    • Rastogi, V.K.1    Girvin, M.E.2
  • 123
    • 0035970046 scopus 로고    scopus 로고
    • Rotation of the c subunit oligomer in fully functional F1F0 ATP synthase
    • S. P. Tsunoda, R. Aggeler, M. Yoshida and R. A. Capaldi, Rotation of the c subunit oligomer in fully functional F1F0 ATP synthase, Proc. Natl. Acad. Sci., 98, 898-902 (2001).
    • (2001) Proc. Natl. Acad. Sci. , vol.98 , pp. 898-902
    • Tsunoda, S.P.1    Aggeler, R.2    Yoshida, M.3    Capaldi, R.A.4
  • 124
    • 0030934380 scopus 로고    scopus 로고
    • Direct observation of the rotation of F1-ATPase
    • H. Noji, R. Yasuda, M. Yoshida and K. J. Kinosita, Direct observation of the rotation of F1-ATPase, Nature, 386, 299-302 (1997).
    • (1997) Nature , vol.386 , pp. 299-302
    • Noji, H.1    Yasuda, R.2    Yoshida, M.3    Kinosita, K.J.4
  • 125
    • 0032568695 scopus 로고    scopus 로고
    • F1-ATPase is a highly efficient molecular motor that rotates with discrete 120° steps
    • R. Yasuda, H. Noji, K. J. Kinosita and M. Yoshida, F1-ATPase is a highly efficient molecular motor that rotates with discrete 120° steps, Cell, 93, 1117-1124 (1998).
    • (1998) Cell , vol.93 , pp. 1117-1124
    • Yasuda, R.1    Noji, H.2    Kinosita, K.J.3    Yoshida, M.4
  • 126
    • 0035912221 scopus 로고    scopus 로고
    • Resolution of distinct rotational sunsteps by submillisecond kinetic analysis of F1-ATPase
    • R. Yasuda, H. Noji, M. Yoshida, K. Kinoshita and H. Itoh, Resolution of distinct rotational sunsteps by submillisecond kinetic analysis of F1-ATPase, Nature, 410, 898-904 (2001).
    • (2001) Nature , vol.410 , pp. 898-904
    • Yasuda, R.1    Noji, H.2    Yoshida, M.3    Kinoshita, K.4    Itoh, H.5
  • 129
    • 0028114231 scopus 로고
    • Structure at 2.8A ° resolution of F1-ATPase from bovine heart mitochondria
    • J. P. Abrahams, A. G. W. Leslie, R. Lutter and J. E. Walker, Structure at 2.8A ° resolution of F1-ATPase from bovine heart mitochondria, Nature, 370, 621-628 (1994).
    • (1994) Nature , vol.370 , pp. 621-628
    • Abrahams, J.P.1    Leslie, A.G.W.2    Lutter, R.3    Walker, J.E.4
  • 130
    • 17844392351 scopus 로고    scopus 로고
    • Nature's rotary electromotors
    • W. Junge and N. Nelson, Nature's rotary electromotors, Science, 308, 642-644 (2005).
    • (2005) Science , vol.308 , pp. 642-644
    • Junge, W.1    Nelson, N.2
  • 131
    • 17844367330 scopus 로고    scopus 로고
    • Structure of the rotor ring of F-type Na{thorn}-ATPase from Ilyobacter tartaricus
    • T. Meier, P. Polzer, K. Diederichs, W. Welte and P. Dimroth, Structure of the rotor ring of F-type Na{thorn}-ATPase from Ilyobacter tartaricus, Science, 308, 659-662 (2005).
    • (2005) Science , vol.308 , pp. 659-662
    • Meier, T.1    Polzer, P.2    Diederichs, K.3    Welte, W.4    Dimroth, P.5
  • 132
    • 17844369968 scopus 로고    scopus 로고
    • Structure of the rotor of the V-type Na{thorn}-ATPase from Enterococcus hirae
    • T. Murata, I. Yanato, Y. Kakinuma, A. G.W. Leslie and J. E. Walker, Structure of the rotor of the V-type Na{thorn}-ATPase from Enterococcus hirae, Science, 308, 564-659 (2005).
    • (2005) Science , vol.308 , pp. 564-659
    • Murata, T.1    Yanato, I.2    Kakinuma, Y.3    Leslie, A.G.W.4    Walker, J.E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.