Spin-density distribution, conformation, and hydrogen bonding of the redox-active tyrosine Y{sub z} in photosystem II from multiple electron magnetic-resonance spectroscopies: Implications for photosynthetic oxygen evolution

doi:https://doi.org/10.1021/ja00146a017

Title: Spin-density distribution, conformation, and hydrogen bonding of the redox-active tyrosine Y{sub z} in photosystem II from multiple electron magnetic-resonance spectroscopies: Implications for photosynthetic oxygen evolution

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Abstract

The oxidized form of the redox-active Y{sub Z} tyrosyl residue involved in photosynthetic oxygen evolution has been generated and trapped in Mn-depleted Photosystem II core complexes from a D2-Y160F mutant strain of Synechocystis 6803. This system eliminates interference from P{sub 700}{sup +} and Y{sub D}D+{center_dot} and allowed characterization of Y{sub Z}{sup {center_dot}} by using a combination of specific {sup 2}H-labeling and electron magnetic-resonance techniques that included CW-EPR, frequency-modulated and transient detected ENDOR, and {sup 2}H-ESEEM. Using these complementary techniques, we have carried out a detailed evaluation of the hyperfine structure of Y{sub Z}{sup {center_dot}} and obtained the dipolar interactions to weakly coupled nuclei, the strongly anisotropic tensors of the ring-hydrogens, and the more isotropic interactions to the {Beta}-methylene site. We conclude that tyrosyl radicals are not tuned to specific function by large-scale modulations of their spin density through hydrogen-bonding effects. We suggest a hydrogen-atom transfer function for Y{sub Z} in water oxidation. Within this model, the (Mn){sub 4}/Y{sub Z} center forms the Oxygen-Evolving Complex of Photosystem II where the (Mn){sub 4} cluster binds substrate water and delocalizes oxidizing equivalents and Y{sub Z} acts by abstracting hydrogens from substrate water in either a concerted or sequential fashion. 71 refs., 8 figs.,more » 2 tabs.« less

Authors:

Tommos, C ^[1]; Tang, X S; Diner, B A ^[2]; Warncke, K; Hoganson, C W; McCracken, J; Babcock, G T ^[3]; Styring, S ^[1]

Stockholm Univ. (Sweden)
E. I. Du Pont deNemours and Co., Wilmington, DE (United States)
Michigan State Univ., East Lansing, MI (United States)

Publication Date:: 1995-10-18

OSTI Identifier:: 136297

Resource Type:: Journal Article

Journal Name:: Journal of the American Chemical Society

Additional Journal Information:: Journal Volume: 117; Journal Issue: 41; Other Information: PBD: 18 Oct 1995

Country of Publication:: United States

Language:: English

Subject:: 55 BIOLOGY AND MEDICINE, BASIC STUDIES; 40 CHEMISTRY; 66 PHYSICS; OXYGEN; PHOTOSYNTHESIS; TYROSINE; REDOX REACTIONS; ENERGY SPECTRA; COMPLEXES; HYDROGEN; PHOTOSYNTHETIC REACTION CENTERS; CHEMICAL BONDS; OXIDATION; ENDOR; ELECTRON SPIN RESONANCE; ELECTRONIC STRUCTURE

Citation Formats


                    Tommos, C, Michigan State Univ., East Lansing, MI, Tang, X S, Diner, B A, Warncke, K, Hoganson, C W, McCracken, J, Babcock, G T, and Styring, S. Spin-density distribution, conformation, and hydrogen bonding of the redox-active tyrosine Y{sub z} in photosystem II from multiple electron magnetic-resonance spectroscopies: Implications for photosynthetic oxygen evolution.  United States: N. p., 1995. 
        Web.  doi:10.1021/ja00146a017.

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                    Tommos, C, Michigan State Univ., East Lansing, MI, Tang, X S, Diner, B A, Warncke, K, Hoganson, C W, McCracken, J, Babcock, G T, & Styring, S. Spin-density distribution, conformation, and hydrogen bonding of the redox-active tyrosine Y{sub z} in photosystem II from multiple electron magnetic-resonance spectroscopies: Implications for photosynthetic oxygen evolution.  United States.  https://doi.org/10.1021/ja00146a017

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                    Tommos, C, Michigan State Univ., East Lansing, MI, Tang, X S, Diner, B A, Warncke, K, Hoganson, C W, McCracken, J, Babcock, G T, and Styring, S. Wed .  
        "Spin-density distribution, conformation, and hydrogen bonding of the redox-active tyrosine Y{sub z} in photosystem II from multiple electron magnetic-resonance spectroscopies: Implications for photosynthetic oxygen evolution".  United States.  https://doi.org/10.1021/ja00146a017.

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@article{osti_136297,

  title        = {Spin-density distribution, conformation, and hydrogen bonding of the redox-active tyrosine Y{sub z} in photosystem II from multiple electron magnetic-resonance spectroscopies: Implications for photosynthetic oxygen evolution},

  author       = {Tommos, C and Michigan State Univ., East Lansing, MI and Tang, X S and Diner, B A and Warncke, K and Hoganson, C W and McCracken, J and Babcock, G T and Styring, S},

  abstractNote = {The oxidized form of the redox-active Y{sub Z} tyrosyl residue involved in photosynthetic oxygen evolution has been generated and trapped in Mn-depleted Photosystem II core complexes from a D2-Y160F mutant strain of Synechocystis 6803. This system eliminates interference from P{sub 700}{sup +} and Y{sub D}D+{center_dot} and allowed characterization of Y{sub Z}{sup {center_dot}} by using a combination of specific {sup 2}H-labeling and electron magnetic-resonance techniques that included CW-EPR, frequency-modulated and transient detected ENDOR, and {sup 2}H-ESEEM. Using these complementary techniques, we have carried out a detailed evaluation of the hyperfine structure of Y{sub Z}{sup {center_dot}} and obtained the dipolar interactions to weakly coupled nuclei, the strongly anisotropic tensors of the ring-hydrogens, and the more isotropic interactions to the {Beta}-methylene site. We conclude that tyrosyl radicals are not tuned to specific function by large-scale modulations of their spin density through hydrogen-bonding effects. We suggest a hydrogen-atom transfer function for Y{sub Z} in water oxidation. Within this model, the (Mn){sub 4}/Y{sub Z} center forms the Oxygen-Evolving Complex of Photosystem II where the (Mn){sub 4} cluster binds substrate water and delocalizes oxidizing equivalents and Y{sub Z} acts by abstracting hydrogens from substrate water in either a concerted or sequential fashion. 71 refs., 8 figs., 2 tabs.},

  doi          = {10.1021/ja00146a017},

  url          = {https://www.osti.gov/biblio/136297},
  journal      = {Journal of the American Chemical Society},
number       = 41,

  volume       = 117,

  place        = {United States},

  year         = {1995},

  month        = {10}

}

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