메뉴 건너뛰기




Volumn 15, Issue 1, 2007, Pages 29-38

Atomic Resolution Structures of Rieske Iron-Sulfur Protein: Role of Hydrogen Bonds in Tuning the Redox Potential of Iron-Sulfur Clusters

Author keywords

[No Author keywords available]

Indexed keywords

IRON SULFUR PROTEIN;

EID: 33846263979     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2006.11.012     Document Type: Article
Times cited : (59)

References (46)
  • 1
    • 0001282755 scopus 로고
    • NH-S hydrogen bonds in Peptococcus aerogenes ferredoxin, Clostridium pasteurianum rubredoxin, and Chromatium high potential iron protein
    • Adman E., Watenpaugh K.D., and Jensen L.H. NH-S hydrogen bonds in Peptococcus aerogenes ferredoxin, Clostridium pasteurianum rubredoxin, and Chromatium high potential iron protein. Proc. Natl. Acad. Sci. USA 72 (1975) 4854-4858
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 4854-4858
    • Adman, E.1    Watenpaugh, K.D.2    Jensen, L.H.3
  • 2
    • 0000590568 scopus 로고
    • Environment of Fe4S4 clusters in ferredoxins and high-potential iron proteins. New information from x-ray crystallography and resonance Raman spectroscopy
    • Backes G., Mino Y., Loehr T.M., Meyer T.E., Cusanovich M.A., Sweeney W.V., Adman E.T., and Sanders-Loefr J. Environment of Fe4S4 clusters in ferredoxins and high-potential iron proteins. New information from x-ray crystallography and resonance Raman spectroscopy. J. Am. Chem. Soc. 113 (1991) 2055-2064
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 2055-2064
    • Backes, G.1    Mino, Y.2    Loehr, T.M.3    Meyer, T.E.4    Cusanovich, M.A.5    Sweeney, W.V.6    Adman, E.T.7    Sanders-Loefr, J.8
  • 5
    • 0036301443 scopus 로고    scopus 로고
    • The structure of the soluble domain of an archaeal Rieske iron-sulfur protein at 1.1 Å resolution
    • Bonisch H., Schmidt C.L., Schafer G., and Ladenstein R. The structure of the soluble domain of an archaeal Rieske iron-sulfur protein at 1.1 Å resolution. J. Mol. Biol. 319 (2002) 791-805
    • (2002) J. Mol. Biol. , vol.319 , pp. 791-805
    • Bonisch, H.1    Schmidt, C.L.2    Schafer, G.3    Ladenstein, R.4
  • 6
    • 0028277764 scopus 로고
    • The protonmotive Q cycle in mitochondria and bacteria
    • Brandt U., and Trumpower B. The protonmotive Q cycle in mitochondria and bacteria. Crit. Rev. Biochem. Mol. Biol. 29 (1994) 165-197
    • (1994) Crit. Rev. Biochem. Mol. Biol. , vol.29 , pp. 165-197
    • Brandt, U.1    Trumpower, B.2
  • 7
    • 0001897686 scopus 로고
    • Assessment of phase accuracy by cross validation: the free R value. Methods and applications
    • Brunger A.T. Assessment of phase accuracy by cross validation: the free R value. Methods and applications. Acta Crystallogr. D Biol. Crystallogr. 49 (1993) 24-36
    • (1993) Acta Crystallogr. D Biol. Crystallogr. , vol.49 , pp. 24-36
    • Brunger, A.T.1
  • 8
    • 0031574021 scopus 로고    scopus 로고
    • Biological identity and diversity in photosynthesis and respiration: structure of the lumen-side domain of the chloroplast Rieske protein
    • Carrell C.J., Zhang H., Cramer W.A., and Smith J.L. Biological identity and diversity in photosynthesis and respiration: structure of the lumen-side domain of the chloroplast Rieske protein. Structure 5 (1997) 1613-1625
    • (1997) Structure , vol.5 , pp. 1613-1625
    • Carrell, C.J.1    Zhang, H.2    Cramer, W.A.3    Smith, J.L.4
  • 9
    • 0030204058 scopus 로고    scopus 로고
    • Wavelets and molecular structure
    • Carson M. Wavelets and molecular structure. J. Comput. Aided Mol. Des. 10 (1996) 273-283
    • (1996) J. Comput. Aided Mol. Des. , vol.10 , pp. 273-283
    • Carson, M.1
  • 10
    • 0000522092 scopus 로고
    • X-ray diffraction studies on chromatium high potential iron protein and on ferredoxin
    • Lovenberg W. (Ed), Academic Press, New York
    • Carter Jr. C.W. X-ray diffraction studies on chromatium high potential iron protein and on ferredoxin. In: Lovenberg W. (Ed). Iron-Sulfur Proteins Volume 3 (1977), Academic Press, New York 157-204
    • (1977) Iron-Sulfur Proteins , vol.3 , pp. 157-204
    • Carter Jr., C.W.1
  • 11
    • 0034480510 scopus 로고    scopus 로고
    • A cluster exposed: structure of the Rieske ferredoxin from biphenyl dioxygenase and the redox properties of Rieske Fe-S proteins
    • Colbert C.L., Couture M.M., Eltis L.D., and Bolin J.T. A cluster exposed: structure of the Rieske ferredoxin from biphenyl dioxygenase and the redox properties of Rieske Fe-S proteins. Structure 8 (2000) 1267-1278
    • (2000) Structure , vol.8 , pp. 1267-1278
    • Colbert, C.L.1    Couture, M.M.2    Eltis, L.D.3    Bolin, J.T.4
  • 12
    • 1942447877 scopus 로고    scopus 로고
    • The cytochrome bc1 complex: function in the context of structure
    • Crofts A.R. The cytochrome bc1 complex: function in the context of structure. Annu. Rev. Physiol. 66 (2004) 689-733
    • (2004) Annu. Rev. Physiol. , vol.66 , pp. 689-733
    • Crofts, A.R.1
  • 13
    • 0032143551 scopus 로고    scopus 로고
    • Structure and function of the cytochrome bc1 complex of mitochondria and photosynthetic bacteria
    • Crofts A.R., and Berry E.A. Structure and function of the cytochrome bc1 complex of mitochondria and photosynthetic bacteria. Curr. Opin. Struct. Biol. 8 (1998) 501-509
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 501-509
    • Crofts, A.R.1    Berry, E.A.2
  • 14
    • 0020173148 scopus 로고
    • A Q-cycle mechanism for the cyclic electron-transfer chain of Rhodopseudomonas sphaeroides
    • Crofts A.R., and Meinhardt S.W. A Q-cycle mechanism for the cyclic electron-transfer chain of Rhodopseudomonas sphaeroides. Biochem. Soc. Trans. 10 (1982) 201-203
    • (1982) Biochem. Soc. Trans. , vol.10 , pp. 201-203
    • Crofts, A.R.1    Meinhardt, S.W.2
  • 16
    • 0001104663 scopus 로고
    • The role of the quinone pool in the cyclic electron-transfer chain of Rhodopseudomonas sphaeroides: a modified Q-cycle mechanism
    • Crofts A.R., Meinhardt S.W., Jones K.R., and Snozzi M. The role of the quinone pool in the cyclic electron-transfer chain of Rhodopseudomonas sphaeroides: a modified Q-cycle mechanism. Biochim. Biophys. Acta. 723 (1983) 202-218
    • (1983) Biochim. Biophys. Acta. , vol.723 , pp. 202-218
    • Crofts, A.R.1    Meinhardt, S.W.2    Jones, K.R.3    Snozzi, M.4
  • 17
    • 0141704297 scopus 로고    scopus 로고
    • The modified Q-cycle explains the apparent mismatch between the kinetics of reduction of cytochromes c1 and bH in the bc1 complex
    • Crofts A.R., Shinkarev V.P., Kolling D.R., and Hong S. The modified Q-cycle explains the apparent mismatch between the kinetics of reduction of cytochromes c1 and bH in the bc1 complex. J. Biol. Chem. 278 (2003) 36191-36201
    • (2003) J. Biol. Chem. , vol.278 , pp. 36191-36201
    • Crofts, A.R.1    Shinkarev, V.P.2    Kolling, D.R.3    Hong, S.4
  • 18
    • 0032502711 scopus 로고    scopus 로고
    • Alteration of the midpoint potential and catalytic activity of the rieske iron-sulfur protein by changes of amino acids forming hydrogen bonds to the iron-sulfur cluster
    • Denke E., Merbitz-Zahradnik T., Hatzfeld O.M., Snyder C.H., Link T.A., and Trumpower B.L. Alteration of the midpoint potential and catalytic activity of the rieske iron-sulfur protein by changes of amino acids forming hydrogen bonds to the iron-sulfur cluster. J. Biol. Chem. 273 (1998) 9085-9093
    • (1998) J. Biol. Chem. , vol.273 , pp. 9085-9093
    • Denke, E.1    Merbitz-Zahradnik, T.2    Hatzfeld, O.M.3    Snyder, C.H.4    Link, T.A.5    Trumpower, B.L.6
  • 19
    • 0037163143 scopus 로고    scopus 로고
    • Photoinduced electron transfer between the Rieske iron-sulfur protein and cytochrome c(1) in the Rhodobacter sphaeroides cytochrome bc(1) complex. Effects of pH, temperature, and driving force
    • Engstrom G., Xiao K., Yu C.A., Yu L., Durham B., and Millett F. Photoinduced electron transfer between the Rieske iron-sulfur protein and cytochrome c(1) in the Rhodobacter sphaeroides cytochrome bc(1) complex. Effects of pH, temperature, and driving force. J. Biol. Chem. 277 (2002) 31072-31078
    • (2002) J. Biol. Chem. , vol.277 , pp. 31072-31078
    • Engstrom, G.1    Xiao, K.2    Yu, C.A.3    Yu, L.4    Durham, B.5    Millett, F.6
  • 20
    • 0033117347 scopus 로고    scopus 로고
    • Expression and one-step purification of a fully active polyhistidine-tagged cytochrome bc1 complex from Rhodobacter sphaeroides
    • Guergova-Kuras M., Salcedo-Hernandez R., Bechmann G., Kuras R., Gennis R.B., and Crofts A.R. Expression and one-step purification of a fully active polyhistidine-tagged cytochrome bc1 complex from Rhodobacter sphaeroides. Protein Expr. Purif. 15 (1999) 370-380
    • (1999) Protein Expr. Purif. , vol.15 , pp. 370-380
    • Guergova-Kuras, M.1    Salcedo-Hernandez, R.2    Bechmann, G.3    Kuras, R.4    Gennis, R.B.5    Crofts, A.R.6
  • 21
    • 0034720770 scopus 로고    scopus 로고
    • Specific mutagenesis of the rieske iron-sulfur protein in Rhodobacter sphaeroides shows that both the thermodynamic gradient and the pK of the oxidized form determine the rate of quinol oxidation by the bc(1) complex
    • Guergova-Kuras M., Kuras R., Ugulava N., Hadad I., and Crofts A.R. Specific mutagenesis of the rieske iron-sulfur protein in Rhodobacter sphaeroides shows that both the thermodynamic gradient and the pK of the oxidized form determine the rate of quinol oxidation by the bc(1) complex. Biochemistry 39 (2000) 7436-7444
    • (2000) Biochemistry , vol.39 , pp. 7436-7444
    • Guergova-Kuras, M.1    Kuras, R.2    Ugulava, N.3    Hadad, I.4    Crofts, A.R.5
  • 22
    • 0033607677 scopus 로고    scopus 로고
    • The energy landscape for ubihydroquinone oxidation at the Q(o) site of the bc(1) complex in Rhodobacter sphaeroides
    • Hong S., Ugulava N., Guergova-Kuras M., and Crofts A.R. The energy landscape for ubihydroquinone oxidation at the Q(o) site of the bc(1) complex in Rhodobacter sphaeroides. J. Biol. Chem. 274 (1999) 33931-33944
    • (1999) J. Biol. Chem. , vol.274 , pp. 33931-33944
    • Hong, S.1    Ugulava, N.2    Guergova-Kuras, M.3    Crofts, A.R.4
  • 24
    • 0030585240 scopus 로고    scopus 로고
    • Structure of a water soluble fragment of the 'Rieske' iron-sulfur protein of the bovine heart mitochondrial cytochrome bc1 complex determined by MAD phasing at 1.5 Å resolution
    • Iwata S., Saynovits M., Link T.A., and Michel H. Structure of a water soluble fragment of the 'Rieske' iron-sulfur protein of the bovine heart mitochondrial cytochrome bc1 complex determined by MAD phasing at 1.5 Å resolution. Structure 4 (1996) 567-579
    • (1996) Structure , vol.4 , pp. 567-579
    • Iwata, S.1    Saynovits, M.2    Link, T.A.3    Michel, H.4
  • 27
    • 18244382074 scopus 로고    scopus 로고
    • Roles of the disulfide bond and adjacent residues in determining the reduction potentials and stabilities of respiratory-type Rieske clusters
    • Leggate E.J., and Hirst J. Roles of the disulfide bond and adjacent residues in determining the reduction potentials and stabilities of respiratory-type Rieske clusters. Biochemistry 44 (2005) 7048-7058
    • (2005) Biochemistry , vol.44 , pp. 7048-7058
    • Leggate, E.J.1    Hirst, J.2
  • 28
    • 0442331120 scopus 로고    scopus 로고
    • The structures of Rieske and Rieske-type proteins
    • Link T.A. The structures of Rieske and Rieske-type proteins. Adv. Inorg. Chem. 47 (1999) 83-157
    • (1999) Adv. Inorg. Chem. , vol.47 , pp. 83-157
    • Link, T.A.1
  • 29
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit-A versatile program for manipulating atomic coordinates and electron density
    • McRee D.E. XtalView/Xfit-A versatile program for manipulating atomic coordinates and electron density. J. Struct. Biol. 125 (1999) 156-165
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 30
    • 0017148721 scopus 로고
    • Possible molecular mechanisms of the protonmotive function of cytochrome systems
    • Mitchell P. Possible molecular mechanisms of the protonmotive function of cytochrome systems. J. Theor. Biol. 62 (1976) 327-367
    • (1976) J. Theor. Biol. , vol.62 , pp. 327-367
    • Mitchell, P.1
  • 31
    • 0347383760 scopus 로고    scopus 로고
    • ARP/wARP and automatic interpretation of protein electron density maps
    • Morris R.J., Perrakis A., and Lamzin V.S. ARP/wARP and automatic interpretation of protein electron density maps. Methods Enzymol. 374 (2003) 229-244
    • (2003) Methods Enzymol. , vol.374 , pp. 229-244
    • Morris, R.J.1    Perrakis, A.2    Lamzin, V.S.3
  • 33
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276 (1997) 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 35
    • 0032127537 scopus 로고    scopus 로고
    • Mutational analysis of residues forming hydrogen bonds in the Rieske [2Fe-2S] cluster of the cytochrome bc1 complex in Paracoccus denitrificans
    • Schroter T., Hatzfeld O.M., Gemeinhardt S., Korn M., Friedrich T., Ludwig B., and Link T.A. Mutational analysis of residues forming hydrogen bonds in the Rieske [2Fe-2S] cluster of the cytochrome bc1 complex in Paracoccus denitrificans. Eur. J. Biochem. 255 (1998) 100-106
    • (1998) Eur. J. Biochem. , vol.255 , pp. 100-106
    • Schroter, T.1    Hatzfeld, O.M.2    Gemeinhardt, S.3    Korn, M.4    Friedrich, T.5    Ludwig, B.6    Link, T.A.7
  • 36
    • 0347383761 scopus 로고    scopus 로고
    • SOLVE and RESOLVE: automated structure solution and density modification
    • Terwilliger T.C. SOLVE and RESOLVE: automated structure solution and density modification. Methods Enzymol. 374 (2003) 22-37
    • (2003) Methods Enzymol. , vol.374 , pp. 22-37
    • Terwilliger, T.C.1
  • 37
    • 0032407459 scopus 로고    scopus 로고
    • CD-monitored redox titration of the Rieske Fe-S protein of Rhodobacter sphaeroides: pH dependence of the midpoint potential in isolated bc1 complex and in membranes
    • Ugulava N.B., and Crofts A.R. CD-monitored redox titration of the Rieske Fe-S protein of Rhodobacter sphaeroides: pH dependence of the midpoint potential in isolated bc1 complex and in membranes. FEBS Lett. 440 (1998) 409-413
    • (1998) FEBS Lett. , vol.440 , pp. 409-413
    • Ugulava, N.B.1    Crofts, A.R.2
  • 38
    • 0034517589 scopus 로고    scopus 로고
    • An approach to multi-copy search in molecular replacement
    • Vagin A., and Teplyakov A. An approach to multi-copy search in molecular replacement. Acta Crystallogr. D Biol. Crystallogr. 56 (2000) 1622-1624
    • (2000) Acta Crystallogr. D Biol. Crystallogr. , vol.56 , pp. 1622-1624
    • Vagin, A.1    Teplyakov, A.2
  • 41
    • 0034624079 scopus 로고    scopus 로고
    • Confirmation of the involvement of protein domain movement during the catalytic cycle of the cytochrome bc1 complex by the formation of an intersubunit disulfide bond between cytochrome b and the iron-sulfur protein
    • Xiao K., Yu L., and Yu C.A. Confirmation of the involvement of protein domain movement during the catalytic cycle of the cytochrome bc1 complex by the formation of an intersubunit disulfide bond between cytochrome b and the iron-sulfur protein. J. Biol. Chem. 275 (2000) 38597-38604
    • (2000) J. Biol. Chem. , vol.275 , pp. 38597-38604
    • Xiao, K.1    Yu, L.2    Yu, C.A.3
  • 42
    • 0025612754 scopus 로고
    • Cloning and DNA sequencing of the fbc operon encoding the cytochrome bc1 complex from Rhodobacter sphaeroides. Characterization of fbc deletion mutants and complementation by a site-specific mutational variant
    • Yun C.H., Beci R., Crofts A.R., Kaplan S., and Gennis R.B. Cloning and DNA sequencing of the fbc operon encoding the cytochrome bc1 complex from Rhodobacter sphaeroides. Characterization of fbc deletion mutants and complementation by a site-specific mutational variant. Eur. J. Biochem. 194 (1990) 399-411
    • (1990) Eur. J. Biochem. , vol.194 , pp. 399-411
    • Yun, C.H.1    Beci, R.2    Crofts, A.R.3    Kaplan, S.4    Gennis, R.B.5
  • 44
    • 0037031281 scopus 로고    scopus 로고
    • Redox properties of the [2Fe-2S] center in the 24 kDa (NQO2) subunit of NADH:ubiquinone oxidoreductase (complex I)
    • Zu Y., Di Bernardo S., Yagi T., and Hirst J. Redox properties of the [2Fe-2S] center in the 24 kDa (NQO2) subunit of NADH:ubiquinone oxidoreductase (complex I). Biochemistry 41 (2002) 10056-10069
    • (2002) Biochemistry , vol.41 , pp. 10056-10069
    • Zu, Y.1    Di Bernardo, S.2    Yagi, T.3    Hirst, J.4
  • 45
    • 0037180385 scopus 로고    scopus 로고
    • Breaking and re-forming the disulfide bond at the high-potential, respiratory-type Rieske [2Fe-2S] center of Thermus thermophilus: characterization of the sulfhydryl state by protein-film voltammetry
    • Zu Y., Fee J.A., and Hirst J. Breaking and re-forming the disulfide bond at the high-potential, respiratory-type Rieske [2Fe-2S] center of Thermus thermophilus: characterization of the sulfhydryl state by protein-film voltammetry. Biochemistry 41 (2002) 14054-14065
    • (2002) Biochemistry , vol.41 , pp. 14054-14065
    • Zu, Y.1    Fee, J.A.2    Hirst, J.3
  • 46
    • 0142063412 scopus 로고    scopus 로고
    • Reduction potentials of Rieske clusters: importance of the coupling between oxidation state and histidine protonation state
    • Zu Y., Couture M.M., Kolling D.R., Crofts A.R., Eltis L.D., Fee J.A., and Hirst J. Reduction potentials of Rieske clusters: importance of the coupling between oxidation state and histidine protonation state. Biochemistry 42 (2003) 12400-12408
    • (2003) Biochemistry , vol.42 , pp. 12400-12408
    • Zu, Y.1    Couture, M.M.2    Kolling, D.R.3    Crofts, A.R.4    Eltis, L.D.5    Fee, J.A.6    Hirst, J.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.