Chemical complementation identifies a proton acceptor for redox-active tyrosine D in photosystem II.

Chemical complementation identifies a proton acceptor for redox-active tyrosine D in photosystem II. Research Abstract Details 

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Chemical complementation identifies a proton acceptor for redox-active tyrosine D in photosystem II. Abstract Text:

S Kim,J Liang,B A Barry,

Through the use of site-directed mutagenesis and chemical rescue, we have identified the proton acceptor for redox-active tyrosine D in photosystem II (PSII). Effects of chemical rescue on the tyrosyl radical were monitored by EPR spectroscopy. We also have acquired the Fourier-transform infrared (FT-IR) spectrum associated with the oxidation of tyrosine D and concomitant protonation of the acceptor. Mutant and isotopically labeled PSII samples are used to assign vibrational lines in the 3,600-3,100 cm-1 region to N-H modes of His-189 in the D2 polypeptide. When His-189 in D2 is changed to a leucine (HL189D2) in PSII, dramatic alterations of both EPR and FT-IR spectra are observed. When imidazole is introduced into HL189D2 samples, results from both EPR and FT-IR spectroscopy argue that imidazole is functionally reconstituted into an accessible pocket and that imidazole acts as a chemical mimic for His-189. Small perturbations of EPR and FT-IR spectra are consistent with access to this pocket in wild-type PSII, as well. Structures of the analogous site in bacterial reaction centers suggest that an accessible pocket, large enough to contain imidazole, is bordered by tyrosine D and His-189 in the D2 polypeptide. These data provide evidence that His-189 in the D2 polypeptide of PSII acts as a proton acceptor for redox-active tyrosine D and that proton transfer to the imidazole ring facilitates the efficient oxidation/reduction of tyrosine D.

Chemical complementation identifies a proton acceptor for redox-active tyrosine D in photosystem II. Publishing Authors By Initials

S Kim,J Liang,BA Barry,

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Chemical complementation identifies a proton acceptor for redox-active tyrosine D in photosystem II. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Proceedings of the National Academy of Sciences of

VOLUME: 94

Page Numbers: 14406-11

Journal Abbreviation: Proc. Natl. Acad. Sci. U.S.A.

ISSN: 0027-8424

DAY: 23

MONTH: Dec

YEAR: 1997

Chemical complementation identifies a proton acceptor for redox-active tyrosine D in photosystem II. Information

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LANGUAGE: eng

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Grant and Affiliation Information for Chemical complementation identifies a proton acceptor for redox-active tyrosine D in photosystem II.

AFFILIATION: Department of Biochemistry, College of Biological Sciences, University of Minnesota, St. Paul, MN 55108-1022, USA.

Country: United States

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MEDLINETA: Proc Natl Acad Sci U S A

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