Document Detail


245 GHz high-field EPR study of tyrosine-D zero and tyrosine-Z zero in mutants of photosystem II.
MedLine Citation:
PMID:  8547247     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
A 245 GHz 8.7 T high-field EPR study of tyrosine-D (TyrD zero) and tyrosine-Z (TyrZ zero) radicals of photosystem II (PSII) from Synechocystis PCC 6803 was carried out. Identical principal g values for the wild-type Synechocystis and spinach TyrD zero showed that the two radicals were in similar electrostatic environments. By contrast, the principal g values of the TyrD zero in the D2-His189Gln mutant of Synechocystis were different from those of the wild-type and spinach radicals and were similar to those of the tyrosyl radical in ribonucleotide reductase. These comparisons indicate that the D2-His189Gln mutant TyrD zero is not hydrogen-bonded or is only weakly so. The HF-EPR spectrum of TyrZ zero was obtained from the D2-Tyr160Phe mutant that lacks TyrD zero. The principal g values were nearly identical to those of the wild-type TyrD zero. The low-field edge of the TyrZ zero spectrum was much broader than at the other two principal g values and was also much broader than the TyrD zero spectrum. From the identical g values and previous work on tyrosyl radical g values [Un S., Atta M., Fontecave, M., & Rutherford, A. W. (1995) J. Am. Chem. Soc. 117, 10713-10719], it was concluded that TyrZ zero, like TyrD zero, is hydrogen-bonded The broadness of the gx component was interpreted as a distribution in strength of the hydrogen-bonding due to disorder in the protein environment about TyrZ zero.
Authors:
S Un; X S Tang; B A Diner
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Biochemistry     Volume:  35     ISSN:  0006-2960     ISO Abbreviation:  Biochemistry     Publication Date:  1996 Jan 
Date Detail:
Created Date:  1996-02-22     Completed Date:  1996-02-22     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  679-84     Citation Subset:  IM    
Affiliation:
URA1290 CNRS, Department Biologie Cellulaire et Moléculaire, CEA-Saclay, Gif-sur-Yvette, France.
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MeSH Terms
Descriptor/Qualifier:
Electron Spin Resonance Spectroscopy
Free Radicals
Hydrogen Bonding
Mutation
Photosynthetic Reaction Center Complex Proteins / chemistry*
Photosystem II Protein Complex
Spectroscopy, Fourier Transform Infrared
Tyrosine / chemistry*
Chemical
Reg. No./Substance:
0/Free Radicals; 0/Photosynthetic Reaction Center Complex Proteins; 0/Photosystem II Protein Complex; 55520-40-6/Tyrosine

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