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Volumn 51, Issue 42, 2012, Pages 8391-8398

Erratum: Temperature invariance of the nitrogenase electron transfer mechanism(Biochemistry (2012) 51:42 (8391-8398) DOI:10.1021/bi301164j);Temperature invariance of the nitrogenase electron transfer mechanism

Author keywords

[No Author keywords available]

Indexed keywords

ARRHENIUS PLOTS; BINARY ALLOYS; ELECTRON TRANSITIONS; EQUILIBRIUM CONSTANTS; IRON; MOLECULES; PROTEINS; RATE CONSTANTS; SPECIFIC HEAT;

EID: 84867796644     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi301438c     Document Type: Erratum
Times cited : (13)

References (23)
  • 2
    • 0024852902 scopus 로고
    • A transient-kinetic study of the nitrogenase of Klebsiella pneumoniae by stopped-flow calorimetry. Comparison with the myosin ATPase
    • Thorneley, R. N. F., Ashby, G., Howarth, J. V., Millar, N. C., and Gutfreund, H. (1989) A transient-kinetic study of the nitrogenase of Klebsiella pneumoniae by stopped-flow calorimetry. Comparison with the myosin ATPase Biochem. J. 264, 657-661
    • (1989) Biochem. J. , vol.264 , pp. 657-661
    • Thorneley, R.N.F.1    Ashby, G.2    Howarth, J.V.3    Millar, N.C.4    Gutfreund, H.5
  • 3
    • 0000703950 scopus 로고    scopus 로고
    • Mechanism of molybdenum nitrogenase
    • Burgess, B. K. and Lowe, D. J. (1996) Mechanism of molybdenum nitrogenase Chem. Rev. 96, 2983-3011
    • (1996) Chem. Rev. , vol.96 , pp. 2983-3011
    • Burgess, B.K.1    Lowe, D.J.2
  • 4
    • 0035942982 scopus 로고    scopus 로고
    • Duplication and extension of the Thorneley and Lowe kinetic model for Klebsiella pneumoniae nitrogenase catalysis using a MATHEMATICA software platform
    • Wilson, P. E., Nyborg, A. C., and Watt, G. D. (2001) Duplication and extension of the Thorneley and Lowe kinetic model for Klebsiella pneumoniae nitrogenase catalysis using a MATHEMATICA software platform Biophys. Chem. 91, 281-304
    • (2001) Biophys. Chem. , vol.91 , pp. 281-304
    • Wilson, P.E.1    Nyborg, A.C.2    Watt, G.D.3
  • 5
    • 77952559475 scopus 로고    scopus 로고
    • Conformational gating of electron transfer from the nitrogenase Fe protein to MoFe protein
    • Danyal, K., Mayweather, D., Dean, D. R., Seefeldt, L. C., and Hoffman, B. M. (2010) Conformational gating of electron transfer from the nitrogenase Fe protein to MoFe protein J. Am. Chem. Soc. 132, 6894-6895
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 6894-6895
    • Danyal, K.1    Mayweather, D.2    Dean, D.R.3    Seefeldt, L.C.4    Hoffman, B.M.5
  • 6
    • 0344187406 scopus 로고
    • Gated electron transfer: When are observed rates controlled by conformational interconversion?
    • Hoffman, B. M. and Ratner, M. R. (1987) Gated electron transfer: When are observed rates controlled by conformational interconversion? J. Am. Chem. Soc. 109, 6237-6243
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 6237-6243
    • Hoffman, B.M.1    Ratner, M.R.2
  • 7
    • 0000842554 scopus 로고
    • Energetics and dynamics of gated reactions: Control of observed rates by conformational interconversion
    • In (Johnson, M. K. King, R. B. Kurtz, D. M. Jr. Kutal, C. Norton, M. L. and Scott, R. A. Eds.) pp, American Chemical Society, Washington, DC.
    • Hoffman, B. M., Ratner, M. A., and Wallin, S. A. (1990) Energetics and dynamics of gated reactions: Control of observed rates by conformational interconversion. In Advances in Chemistry (Johnson, M. K., King, R. B., Kurtz, D. M., Jr., Kutal, C., Norton, M. L., and Scott, R. A., Eds.) pp 125-146, American Chemical Society, Washington, DC.
    • (1990) Advances in Chemistry , pp. 125-146
    • Hoffman, B.M.1    Ratner, M.A.2    Wallin, S.A.3
  • 8
    • 23944500884 scopus 로고    scopus 로고
    • Nitrogenase complexes: Multiple docking sites for a nucleotide switch protein
    • Tezcan, F. A., Kaiser, J. T., Mustafi, D., Walton, M. Y., Howard, J. B., and Rees, D. C. (2005) Nitrogenase complexes: Multiple docking sites for a nucleotide switch protein Science 309, 1377-1380
    • (2005) Science , vol.309 , pp. 1377-1380
    • Tezcan, F.A.1    Kaiser, J.T.2    Mustafi, D.3    Walton, M.Y.4    Howard, J.B.5    Rees, D.C.6
  • 10
    • 77955344995 scopus 로고    scopus 로고
    • Surface residues dynamically organize water bridges to enhance electron transfer between proteins
    • de la Lande, A., Babcock, N. S., Rezac, J., Sanders, B. C., and Salahub, D. R. (2010) Surface residues dynamically organize water bridges to enhance electron transfer between proteins Proc. Natl. Acad. Sci. U.S.A. 107, 11799-11804
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 11799-11804
    • De La Lande, A.1    Babcock, N.S.2    Rezac, J.3    Sanders, B.C.4    Salahub, D.R.5
  • 11
    • 84867031460 scopus 로고    scopus 로고
    • Interfacial hydration, dynamics and electron transfer: Multi-scale et modeling of the transient [Myoglobin, Cytochrome b5] complex
    • Keinan, S., Nocek, J. M., Hoffman, B. M., and Beratan, D. N. (2012) Interfacial hydration, dynamics and electron transfer: Multi-scale ET modeling of the transient [Myoglobin, Cytochrome b5] complex Phys. Chem. Chem. Phys. 14, 13881-13889
    • (2012) Phys. Chem. Chem. Phys. , vol.14 , pp. 13881-13889
    • Keinan, S.1    Nocek, J.M.2    Hoffman, B.M.3    Beratan, D.N.4
  • 12
    • 80054972869 scopus 로고    scopus 로고
    • Electron transfer within nitrogenase: Evidence for a deficit-spending mechanism
    • Danyal, K., Dean, D. R., Hoffman, B. M., and Seefeldt, L. C. (2011) Electron transfer within nitrogenase: Evidence for a deficit-spending mechanism Biochemistry 50, 9255-9263
    • (2011) Biochemistry , vol.50 , pp. 9255-9263
    • Danyal, K.1    Dean, D.R.2    Hoffman, B.M.3    Seefeldt, L.C.4
  • 13
    • 0345863723 scopus 로고    scopus 로고
    • Structure of multidrug-resistance proteins of the ATP-binding cassette (ABC) superfamily
    • Altenberg, G. A. (2004) Structure of multidrug-resistance proteins of the ATP-binding cassette (ABC) superfamily Curr. Med. Chem.: Anti-Cancer Agents 4, 53-62
    • (2004) Curr. Med. Chem.: Anti-Cancer Agents , vol.4 , pp. 53-62
    • Altenberg, G.A.1
  • 14
    • 0001718603 scopus 로고
    • ATP hydrolysis and energy transduction by nitrogenase
    • In (Tikhonovich, I. A. Provorov, N. A. Romanov, V. I. and Newton, W. E. Eds.) pp, Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • Lowe, D. J., Ashby, G. A., Brune, M., Knights, H., Webb, M. R., and Thorneley, R. N. F. (1995) ATP hydrolysis and energy transduction by nitrogenase. In Nitrogen Fixation: Fundamentals and Applications (Tikhonovich, I. A., Provorov, N. A., Romanov, V. I., and Newton, W. E., Eds.) pp 103-108, Kluwer Academic Publishers, Dordrecht, The Netherlands.
    • (1995) Nitrogen Fixation: Fundamentals and Applications , pp. 103-108
    • Lowe, D.J.1    Ashby, G.A.2    Brune, M.3    Knights, H.4    Webb, M.R.5    Thorneley, R.N.F.6
  • 15
    • 0026612825 scopus 로고
    • Temperature effects on the magnesium-ATP-induced electron transfer between the nitrogenase proteins from Azotobacter vinelandii
    • Mensink, R. E. and Haaker, H. (1992) Temperature effects on the magnesium-ATP-induced electron transfer between the nitrogenase proteins from Azotobacter vinelandii Eur. J. Biochem. 208, 295-299
    • (1992) Eur. J. Biochem. , vol.208 , pp. 295-299
    • Mensink, R.E.1    Haaker, H.2
  • 16
    • 0032488605 scopus 로고    scopus 로고
    • Electron transfer in nitrogenase analyzed by Marcus theory: Evidence for gating by MgATP
    • Lanzilotta, W. N., Parker, V. D., and Seefeldt, L. C. (1998) Electron transfer in nitrogenase analyzed by Marcus theory: Evidence for gating by MgATP Biochemistry 37, 399-407
    • (1998) Biochemistry , vol.37 , pp. 399-407
    • Lanzilotta, W.N.1    Parker, V.D.2    Seefeldt, L.C.3
  • 17
    • 0032497358 scopus 로고    scopus 로고
    • Catalytic and biophysical properties of a nitrogenase apo-MoFe protein produced by a nifB-deletion mutant of Azotobacter vinelandii
    • Christiansen, J., Goodwin, P. J., Lanzilotta, W. N., Seefeldt, L. C., and Dean, D. R. (1998) Catalytic and biophysical properties of a nitrogenase apo-MoFe protein produced by a nifB-deletion mutant of Azotobacter vinelandii Biochemistry 37, 12611-12623
    • (1998) Biochemistry , vol.37 , pp. 12611-12623
    • Christiansen, J.1    Goodwin, P.J.2    Lanzilotta, W.N.3    Seefeldt, L.C.4    Dean, D.R.5
  • 18
    • 0019321298 scopus 로고
    • Large-scale purification of high activity Azotobacter vinelandii nitrogenase
    • Burgess, B. K., Jacobs, D. B., and Stiefel, E. I. (1980) Large-scale purification of high activity Azotobacter vinelandii nitrogenase Biochim. Biophys. Acta 614, 196-209
    • (1980) Biochim. Biophys. Acta , vol.614 , pp. 196-209
    • Burgess, B.K.1    Jacobs, D.B.2    Stiefel, E.I.3
  • 19
    • 0026713681 scopus 로고
    • Mapping the site(s) of MgATP and MgADP interaction with the nitrogenase of Azotobacter vinelandii. Lysine 15 of the iron protein plays a major role in MgATP interaction
    • Seefeldt, L. C., Morgan, T. V., Dean, D. R., and Mortenson, L. E. (1992) Mapping the site(s) of MgATP and MgADP interaction with the nitrogenase of Azotobacter vinelandii. Lysine 15 of the iron protein plays a major role in MgATP interaction J. Biol. Chem. 267, 6680-6688
    • (1992) J. Biol. Chem. , vol.267 , pp. 6680-6688
    • Seefeldt, L.C.1    Morgan, T.V.2    Dean, D.R.3    Mortenson, L.E.4
  • 20
    • 0029929865 scopus 로고    scopus 로고
    • Evidence for electron transfer from the nitrogenase iron protein to the molybdenum-iron protein without MgATP hydrolysis: Characterization of a tight protein-protein complex
    • Lanzilotta, W. N., Fisher, K., and Seefeldt, L. C. (1996) Evidence for electron transfer from the nitrogenase iron protein to the molybdenum-iron protein without MgATP hydrolysis: Characterization of a tight protein-protein complex Biochemistry 35, 7188-7196
    • (1996) Biochemistry , vol.35 , pp. 7188-7196
    • Lanzilotta, W.N.1    Fisher, K.2    Seefeldt, L.C.3
  • 22
    • 0001442098 scopus 로고
    • Kinetics and mechanism of the nitrogenase enzyme system
    • In (Spiro, T. G. Ed.) pp, Wiley-Interscience, New York.
    • Thorneley, R. N. F. and Lowe, D. J. (1985) Kinetics and mechanism of the nitrogenase enzyme system. In Molybdenum Enzymes (Spiro, T. G., Ed.) pp 89-116, Wiley-Interscience, New York.
    • (1985) Molybdenum Enzymes , pp. 89-116
    • Thorneley, R.N.F.1    Lowe, D.J.2
  • 23
    • 0029130871 scopus 로고
    • Macromolecules and water: Probing with osmotic stress
    • Parsegian, V. A., Rand, R. P., and Rau, D. C. (1995) Macromolecules and water: Probing with osmotic stress Methods Enzymol. 259, 43-94
    • (1995) Methods Enzymol. , vol.259 , pp. 43-94
    • Parsegian, V.A.1    Rand, R.P.2    Rau, D.C.3


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