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Effects of single a...
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Ivković-Jensen, Maja M.Department of Chemistry, Iowa State University, Ames, United States
(författare)
Effects of single and double mutations in plastocyanin on the rate constant and activation parameters for the rearrangement gating the electron-transfer reaction between the triplet state of zinc cytochrome c and cupriplastocyanin
- Artikel/kapitelEngelska1998
Förlag, utgivningsår, omfång ...
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1998-06-11
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American Chemical Society (ACS),1998
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printrdacarrier
Nummerbeteckningar
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LIBRIS-ID:oai:DiVA.org:his-9903
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https://urn.kb.se/resolve?urn=urn:nbn:se:his:diva-9903URI
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https://doi.org/10.1021/bi9802871DOI
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Språk:engelska
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Sammanfattning på:engelska
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Ämneskategori:ref swepub-contenttype
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Ämneskategori:art swepub-publicationtype
Anmärkningar
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The unimolecular rate constant for the photoinduced electron-transfer reaction 3Zncyt/pc(II) --> Zncyt+/pc(I) within the electrostatic complex of zinc cytochrome c and spinach cupriplastocyanin is kF. We report the effects on kF of the following factors, all at pH 7.0: 12 single mutations on the plastocyanin surface (Leu12Asn, Leu12Glu, Leu12Lys, Asp42Asn, Asp42Lys, Glu43Asn, Glu59Gln, Glu59Lys, Glu60Gln, Glu60Lys, Gln88Glu, and Gln88Lys), the double mutation Glu59Lys/Glu60Gln, temperature (in the range 273.3-302.9 K), and solution viscosity (in the range 1. 00-116.0 cP) at 283.2 and 293.2 K. We also report the effects of the plastocyanin mutations on the association constant (Ka) and the corresponding free energy of association (DeltaGa) with zinc cytochrome c at 298.2 K. Dependence of kF on temperature yielded the activation parameters DeltaH, DeltaS, and DeltaG. Dependence of kF on solution viscosity yielded the protein friction and confirmed the DeltaG values determined from the temperature dependence. The aforementioned intracomplex reaction is not a simple electron-transfer reaction because donor-acceptor electronic coupling (HAB) and reorganizational energy (lambda), obtained by fitting of the temperature dependence of kF to the Marcus equation, deviate from the expectations based on precedents and because kF greatly depends on viscosity. This last dependence and the fact that certain mutations affect Ka but not kF are two lines of evidence against the mechanism in which the electron-transfer step is coupled with the faster, but thermodynamically unfavorable, rearrangement step. The electron-transfer reaction is gated by the slower, and thus rate determining, structural rearrangement of the diprotein complex; the rate constant kF corresponds to this rearrangement. Isokinetic correlation of DeltaH and DeltaS parameters and Coulombic energies of the various configurations of the Zncyt/pc(II) complex consistently show that the rearrangement is a facile configurational fluctuation of the associated proteins, qualitatively the same process regardless of the mutations in plastocyanin. Correlation of kF with the orientation of the cupriplastocyanin dipole moment indicates that the reactive configuration of the diprotein complex involves the area near the residue 59, between the upper acidic cluster and the hydrophobic patch. Kinetic effects and noneffects of plastocyanin mutations show that the rearrangement from the initial (docking) configuration, which involves both acidic clusters, to the reactive configuration does not involve the lower acidic cluster and the hydrophobic patch but involves the upper acidic cluster and the area near the residue 88.
Ämnesord och genrebeteckningar
Biuppslag (personer, institutioner, konferenser, titlar ...)
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Ullmann, G. MatthiasInstitut für Kristallographie, Freie Universität Berlin, Germany
(författare)
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Young, SimonDepartment of Biochemistry and Biophysics, Göteborg University, Chalmers University of Technology, Göteborg, Sweden
(författare)
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Hansson, ÖrjanDepartment of Biochemistry and Biophysics, Göteborg University, Chalmers University of Technology, Göteborg, Sweden
(författare)
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Crnogorac, Milan M.Department of Chemistry, Iowa State University, Ames, United States
(författare)
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Ejdebäck, Mikael,1969-Department of Biochemistry and Biophysics, Göteborg University, Chalmers University of Technology, Göteborg, Sweden(Swepub:his)ejdm
(författare)
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Kostić, Nenad M.Department of Chemistry, Iowa State University, Ames, United States
(författare)
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Department of Chemistry, Iowa State University, Ames, United StatesInstitut für Kristallographie, Freie Universität Berlin, Germany
(creator_code:org_t)
Sammanhörande titlar
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Ingår i:Biochemistry: American Chemical Society (ACS)37:26, s. 9557-95690006-29601520-4995
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