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Volumn 52, Issue 17, 2013, Pages 2862-2873

Electron transfer mechanism of the rieske protein from Thermus thermophilus from solution nuclear magnetic resonance investigations

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL SHIFT PERTURBATIONS; CONFORMATIONAL CHANGE; DODECYL PHOSPHOCHOLINE MICELLES; ELECTRON TRANSFER MECHANISMS; IRON-SULFUR CLUSTERS; NUCLEAR MAGNETIC RESONANCE(NMR); PROTEIN CONFORMATION; THERMUS THERMOPHILUS;

EID: 84877025583     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi400296c     Document Type: Article
Times cited : (5)

References (32)
  • 1
    • 33846294004 scopus 로고    scopus 로고
    • Fe-S Rieske center
    • In (Albrecht Messerschmidt, R. H. Wieghardt, K. and Poulos, T. Eds.) pp, Wiley, New York.
    • Link, T. A. (2001) Fe-S Rieske center. In Handbook of Metalloproteins (Albrecht Messerschmidt, R. H., Wieghardt, K., and Poulos, T., Eds.) pp 518-531, Wiley, New York.
    • (2001) Handbook of Metalloproteins , pp. 518-531
    • Link, T.A.1
  • 2
    • 77953318055 scopus 로고    scopus 로고
    • 1 complex
    • In (Albrecht Messerschmidt, R. H. Wieghardt, K. and Poulos, T. Eds.) pp, Wiley, New York.
    • 1 complex. In Handbook of Metalloproteins (Albrecht Messerschmidt, R. H., Wieghardt, K., and Poulos, T., Eds.) pp 402-423, Wiley, New York.
    • (2001) Handbook of Metalloproteins , pp. 402-423
    • Link, T.A.1
  • 5
    • 33748985025 scopus 로고    scopus 로고
    • The menaquinol-oxidizing cytochrome bc complex from Thermus thermophilus: Protein domains and subunits
    • Mooser, D., Maneg, O., MacMillan, F., Malatesta, F., Soulimane, T., and Ludwig, B. (2006) The menaquinol-oxidizing cytochrome bc complex from Thermus thermophilus: Protein domains and subunits Biochim. Biophys. Acta 1757, 1084-1095
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 1084-1095
    • Mooser, D.1    Maneg, O.2    MacMillan, F.3    Malatesta, F.4    Soulimane, T.5    Ludwig, B.6
  • 7
    • 0017148721 scopus 로고
    • Possible molecular mechanisms of the protonmotive function of cytochrome systems
    • Mitchell, P. (1976) Possible molecular mechanisms of the protonmotive function of cytochrome systems J. Theor. Biol. 62, 327-367
    • (1976) J. Theor. Biol. , vol.62 , pp. 327-367
    • Mitchell, P.1
  • 8
    • 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. (2003) 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, 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
  • 11
    • 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. (2000) 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, 38597-38604
    • (2000) J. Biol. Chem. , vol.275 , pp. 38597-38604
    • Xiao, K.1    Yu, L.2    Yu, C.A.3
  • 13
    • 0032311167 scopus 로고    scopus 로고
    • The chemistry and mechanics of ubihydroquinone oxidation at center P (Qo) of the cytochrome bc1 complex
    • Brandt, U. (1998) The chemistry and mechanics of ubihydroquinone oxidation at center P (Qo) of the cytochrome bc1 complex Biochim. Biophys. Acta 1365, 261-268
    • (1998) Biochim. Biophys. Acta , vol.1365 , pp. 261-268
    • Brandt, U.1
  • 18
    • 33748913718 scopus 로고    scopus 로고
    • Proton pumping in the bc1 complex: A new gating mechanism that prevents short circuits
    • Crofts, A. R., Lhee, S., Crofts, S. B., Cheng, J., and Rose, S. (2006) Proton pumping in the bc1 complex: A new gating mechanism that prevents short circuits Biochim. Biophys. Acta 1757, 1019-1034
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 1019-1034
    • Crofts, A.R.1    Lhee, S.2    Crofts, S.B.3    Cheng, J.4    Rose, S.5
  • 20
    • 77951666856 scopus 로고    scopus 로고
    • Prediction of Xaa-Pro peptide bond conformation from sequence and chemical shifts
    • Shen, Y. and Bax, A. (2010) Prediction of Xaa-Pro peptide bond conformation from sequence and chemical shifts J. Biomol. NMR 46, 199-204
    • (2010) J. Biomol. NMR , vol.46 , pp. 199-204
    • Shen, Y.1    Bax, A.2
  • 22
    • 0028889024 scopus 로고
    • Protein expression, selective isotopic labeling, and analysis of hyperfine-shifted NMR signals of Anabaena 7120 vegetative [2Fe-2S]ferredoxin
    • Cheng, H., Westler, W. M., Xia, B., Oh, B. H., and Markley, J. L. (1995) Protein expression, selective isotopic labeling, and analysis of hyperfine-shifted NMR signals of Anabaena 7120 vegetative [2Fe-2S]ferredoxin Arch. Biochem. Biophys. 316, 619-634
    • (1995) Arch. Biochem. Biophys. , vol.316 , pp. 619-634
    • Cheng, H.1    Westler, W.M.2    Xia, B.3    Oh, B.H.4    Markley, J.L.5
  • 24
    • 84890548038 scopus 로고    scopus 로고
    • http://www.cgl.ucsf.edu/home/sparky.
  • 25
    • 0037012374 scopus 로고    scopus 로고
    • 13C} 2D NMR: A Novel Strategy for the Study of Paramagnetic Proteins with Slow Electronic Relaxation Rates
    • 13C} 2D NMR: A Novel Strategy for the Study of Paramagnetic Proteins with Slow Electronic Relaxation Rates J. Am. Chem. Soc. 124, 3204-3205
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 3204-3205
    • MacHonkin, T.E.1    Westler, W.M.2    Markley, J.L.3
  • 26
    • 2342512067 scopus 로고    scopus 로고
    • Strategy for the study of paramagnetic proteins with slow electronic relaxation rates by NMR spectroscopy: Application to oxidized human [2Fe-2S] ferredoxin
    • Machonkin, T. E., Westler, W. M., and Markley, J. L. (2004) Strategy for the study of paramagnetic proteins with slow electronic relaxation rates by NMR spectroscopy: Application to oxidized human [2Fe-2S] ferredoxin J. Am. Chem. Soc. 126, 5413-5426
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 5413-5426
    • MacHonkin, T.E.1    Westler, W.M.2    Markley, J.L.3
  • 27
    • 47749126543 scopus 로고    scopus 로고
    • Structure of complex III with bound cytochrome c in reduced state and definition of a minimal core interface for electron transfer
    • Solmaz, S. R. and Hunte, C. (2008) Structure of complex III with bound cytochrome c in reduced state and definition of a minimal core interface for electron transfer J. Biol. Chem. 283, 17542-17549
    • (2008) J. Biol. Chem. , vol.283 , pp. 17542-17549
    • Solmaz, S.R.1    Hunte, C.2
  • 30
    • 77953296900 scopus 로고    scopus 로고
    • NMR Investigations of the Rieske Protein from Thermus thermophilus Support a Coupled Proton and Electron Transfer Mechanism
    • Hsueh, K. L., Westler, W. M., and Markley, J. L. (2010) NMR Investigations of the Rieske Protein from Thermus thermophilus Support a Coupled Proton and Electron Transfer Mechanism J. Am. Chem. Soc. 132, 7908-7918
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 7908-7918
    • Hsueh, K.L.1    Westler, W.M.2    Markley, J.L.3
  • 31
    • 0035840956 scopus 로고    scopus 로고
    • (1)-type Rieske [2Fe-2S] center of Thermus thermophilus
    • (1)-type Rieske [2Fe-2S] center of Thermus thermophilus J. Am. Chem. Soc. 123, 9906-9907
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 9906-9907
    • Zu, Y.1    Fee, J.A.2    Hirst, J.3
  • 32
    • 33747797654 scopus 로고    scopus 로고
    • 15N NMR titration study demonstrates the role of iron-ligated histidines in the pH dependence of the reduction potential
    • 15N NMR titration study demonstrates the role of iron-ligated histidines in the pH dependence of the reduction potential J. Am. Chem. Soc. 128, 10672-10673
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 10672-10673
    • Lin, I.J.1    Chen, Y.2    Fee, J.A.3    Song, J.4    Westler, W.M.5    Markley, J.L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.