Electron Transfer on the Donor and Acceptor Sides of Photosystem II Explored by Site-Directed Mutagenesis and Kinetic Spectroscopy
Kanazawa, Atsuko
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https://hdl.handle.net/2142/85481
Description
Title
Electron Transfer on the Donor and Acceptor Sides of Photosystem II Explored by Site-Directed Mutagenesis and Kinetic Spectroscopy
Author(s)
Kanazawa, Atsuko
Issue Date
1997
Doctoral Committee Chair(s)
Crofts, Antony R.
Department of Study
Biophysics and Computational Biology
Discipline
Biophysics and Computational Biology
Degree Granting Institution
University of Illinois at Urbana-Champaign
Degree Name
Ph.D.
Degree Level
Dissertation
Keyword(s)
Biology, Plant Physiology
Language
eng
Abstract
H252Q and six donor-side mutants became the important tools to investigate a new model of neutral tyrosine radical, $\rm Y\sb{Z}\sp\cdot,$ introduced by Gilchrist et al. (1995) and Hoganson et al. (1995). In this new model, $\rm Y\sb{Z}$ is not simply a redox active residue in the electron transfer reactions, but is also directly involved in the water-oxidation. The models are critically-dependent on the presence of a neutral radical form of $\rm Y\sb{Z}\ (Y\sb{Z}\sp{\cdot}).$ The donor-side mutants, $\rm E189 > L,Q,$ and $\rm N191 > A,D,L,$ had only small effects on the pH-dependence of the rate of Q$\rm\sb{A}\sp-$ and oxidized $\rm Y\sb{Z}$ recombination. On the other hand, E189D mutant showed a pH-independent in rate of $\rm Q\sb{A}\sp-$ and oxidized $\rm Y\sb{Z}$ recombination. Based on these data, a simple thermodynamic model was introduced to explain the results and the model of $\rm Y\sb{Z}\sp{\cdot}$ as an oxidized form.
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