The function of D1-H332 in Photosystem II electron transport studied by thermoluminescence and chlorophyll fluorescence in site-directed mutants of Synechocystis 6803

Yagut Allahverdiyeva, Z. Deák, András Szilárd, Bruce A. Diner, Peter J. Nixon, I. Vass

Research output: Contribution to journalArticle

36 Citations (Scopus)

Abstract

The His332 residue of the D1 protein has been identified as the likely ligand of the catalytic Mn ions in the water oxidizing complex (Ferreira, K.N., Iverson, T.M., Maghlaoui, K., Barber, J. & Iwata, S. (2004) Science 303, 1831-1838). However, its function has not been fully clarified. Here we used thermoluminescence and flash-induced chlorophyll fluorescence measurements to characterize the effect of the D1-H333E, D1-H332D and D1-H332S mutations on the electron transport of Photosystem II in intact cells of the cyanobacterium Synechocystis 6803. Although the mutants are not photoautotrophic they all show flash-induced thermoluminescence and chlorophyll fluorescence, which originate from the S2QA - and S2Q B - recombinations demonstrating that charge stabilization takes place in the water oxidizing complex. However, the conversion of S 2 to higher S states is inhibited and the energetic stability of the S2QA - charge pair is increased by 75, 50 and 7 mV in the D1-H332D, D1-H332E and D1-H332S mutants, respectively. This is most probably caused by a decrease of Em(S2/S1). Concomitantly, the rate of electron donation from Mn to Tyr-Z. during the S1 to S2 transition is slowed down, relative to the wild type, 350- and 60-fold in the D1-H332E and D1-H332D mutants, respectively, but remains essentially unaffected in D1-H332S. A further effect of the D1-H332E and D1-H332D mutations is the retardation of the QA to QB electron transfer step as an indirect consequence of the donor side modification. Our data show that although the His residue in the D1-332 position can be substituted by other metal binding residues for binding photo-oxidisable Mn it is required for controlling the functional redox energetics of the Mn cluster.

Original languageEnglish
Pages (from-to)3523-3532
Number of pages10
JournalEuropean Journal of Biochemistry
Volume271
Issue number17
DOIs
Publication statusPublished - Sep 2004

Fingerprint

Synechocystis
Thermoluminescence
Photosystem II Protein Complex
Chlorophyll
Electron Transport
Fluorescence
Electrons
Mutation
Water
Cyanobacteria
Genetic Recombination
Oxidation-Reduction
Stabilization
Metals
Ions
Ligands
Proteins

Keywords

  • D1-protein
  • Flash-induced chlorophyll fluorescence
  • His332 mutants
  • Photosystem II
  • Thermoluminescence

ASJC Scopus subject areas

  • Biochemistry

Cite this

The function of D1-H332 in Photosystem II electron transport studied by thermoluminescence and chlorophyll fluorescence in site-directed mutants of Synechocystis 6803. / Allahverdiyeva, Yagut; Deák, Z.; Szilárd, András; Diner, Bruce A.; Nixon, Peter J.; Vass, I.

In: European Journal of Biochemistry, Vol. 271, No. 17, 09.2004, p. 3523-3532.

Research output: Contribution to journalArticle

@article{ec59f8e643a148edb1c547123389c4b3,
title = "The function of D1-H332 in Photosystem II electron transport studied by thermoluminescence and chlorophyll fluorescence in site-directed mutants of Synechocystis 6803",
abstract = "The His332 residue of the D1 protein has been identified as the likely ligand of the catalytic Mn ions in the water oxidizing complex (Ferreira, K.N., Iverson, T.M., Maghlaoui, K., Barber, J. & Iwata, S. (2004) Science 303, 1831-1838). However, its function has not been fully clarified. Here we used thermoluminescence and flash-induced chlorophyll fluorescence measurements to characterize the effect of the D1-H333E, D1-H332D and D1-H332S mutations on the electron transport of Photosystem II in intact cells of the cyanobacterium Synechocystis 6803. Although the mutants are not photoautotrophic they all show flash-induced thermoluminescence and chlorophyll fluorescence, which originate from the S2QA - and S2Q B - recombinations demonstrating that charge stabilization takes place in the water oxidizing complex. However, the conversion of S 2 to higher S states is inhibited and the energetic stability of the S2QA - charge pair is increased by 75, 50 and 7 mV in the D1-H332D, D1-H332E and D1-H332S mutants, respectively. This is most probably caused by a decrease of Em(S2/S1). Concomitantly, the rate of electron donation from Mn to Tyr-Z. during the S1 to S2 transition is slowed down, relative to the wild type, 350- and 60-fold in the D1-H332E and D1-H332D mutants, respectively, but remains essentially unaffected in D1-H332S. A further effect of the D1-H332E and D1-H332D mutations is the retardation of the QA to QB electron transfer step as an indirect consequence of the donor side modification. Our data show that although the His residue in the D1-332 position can be substituted by other metal binding residues for binding photo-oxidisable Mn it is required for controlling the functional redox energetics of the Mn cluster.",
keywords = "D1-protein, Flash-induced chlorophyll fluorescence, His332 mutants, Photosystem II, Thermoluminescence",
author = "Yagut Allahverdiyeva and Z. De{\'a}k and Andr{\'a}s Szil{\'a}rd and Diner, {Bruce A.} and Nixon, {Peter J.} and I. Vass",
year = "2004",
month = "9",
doi = "10.1111/j.0014-2956.2004.04287.x",
language = "English",
volume = "271",
pages = "3523--3532",
journal = "FEBS Journal",
issn = "1742-464X",
publisher = "Wiley-Blackwell",
number = "17",

}

TY - JOUR

T1 - The function of D1-H332 in Photosystem II electron transport studied by thermoluminescence and chlorophyll fluorescence in site-directed mutants of Synechocystis 6803

AU - Allahverdiyeva, Yagut

AU - Deák, Z.

AU - Szilárd, András

AU - Diner, Bruce A.

AU - Nixon, Peter J.

AU - Vass, I.

PY - 2004/9

Y1 - 2004/9

N2 - The His332 residue of the D1 protein has been identified as the likely ligand of the catalytic Mn ions in the water oxidizing complex (Ferreira, K.N., Iverson, T.M., Maghlaoui, K., Barber, J. & Iwata, S. (2004) Science 303, 1831-1838). However, its function has not been fully clarified. Here we used thermoluminescence and flash-induced chlorophyll fluorescence measurements to characterize the effect of the D1-H333E, D1-H332D and D1-H332S mutations on the electron transport of Photosystem II in intact cells of the cyanobacterium Synechocystis 6803. Although the mutants are not photoautotrophic they all show flash-induced thermoluminescence and chlorophyll fluorescence, which originate from the S2QA - and S2Q B - recombinations demonstrating that charge stabilization takes place in the water oxidizing complex. However, the conversion of S 2 to higher S states is inhibited and the energetic stability of the S2QA - charge pair is increased by 75, 50 and 7 mV in the D1-H332D, D1-H332E and D1-H332S mutants, respectively. This is most probably caused by a decrease of Em(S2/S1). Concomitantly, the rate of electron donation from Mn to Tyr-Z. during the S1 to S2 transition is slowed down, relative to the wild type, 350- and 60-fold in the D1-H332E and D1-H332D mutants, respectively, but remains essentially unaffected in D1-H332S. A further effect of the D1-H332E and D1-H332D mutations is the retardation of the QA to QB electron transfer step as an indirect consequence of the donor side modification. Our data show that although the His residue in the D1-332 position can be substituted by other metal binding residues for binding photo-oxidisable Mn it is required for controlling the functional redox energetics of the Mn cluster.

AB - The His332 residue of the D1 protein has been identified as the likely ligand of the catalytic Mn ions in the water oxidizing complex (Ferreira, K.N., Iverson, T.M., Maghlaoui, K., Barber, J. & Iwata, S. (2004) Science 303, 1831-1838). However, its function has not been fully clarified. Here we used thermoluminescence and flash-induced chlorophyll fluorescence measurements to characterize the effect of the D1-H333E, D1-H332D and D1-H332S mutations on the electron transport of Photosystem II in intact cells of the cyanobacterium Synechocystis 6803. Although the mutants are not photoautotrophic they all show flash-induced thermoluminescence and chlorophyll fluorescence, which originate from the S2QA - and S2Q B - recombinations demonstrating that charge stabilization takes place in the water oxidizing complex. However, the conversion of S 2 to higher S states is inhibited and the energetic stability of the S2QA - charge pair is increased by 75, 50 and 7 mV in the D1-H332D, D1-H332E and D1-H332S mutants, respectively. This is most probably caused by a decrease of Em(S2/S1). Concomitantly, the rate of electron donation from Mn to Tyr-Z. during the S1 to S2 transition is slowed down, relative to the wild type, 350- and 60-fold in the D1-H332E and D1-H332D mutants, respectively, but remains essentially unaffected in D1-H332S. A further effect of the D1-H332E and D1-H332D mutations is the retardation of the QA to QB electron transfer step as an indirect consequence of the donor side modification. Our data show that although the His residue in the D1-332 position can be substituted by other metal binding residues for binding photo-oxidisable Mn it is required for controlling the functional redox energetics of the Mn cluster.

KW - D1-protein

KW - Flash-induced chlorophyll fluorescence

KW - His332 mutants

KW - Photosystem II

KW - Thermoluminescence

UR - http://www.scopus.com/inward/record.url?scp=4544283273&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=4544283273&partnerID=8YFLogxK

U2 - 10.1111/j.0014-2956.2004.04287.x

DO - 10.1111/j.0014-2956.2004.04287.x

M3 - Article

C2 - 15317587

AN - SCOPUS:4544283273

VL - 271

SP - 3523

EP - 3532

JO - FEBS Journal

JF - FEBS Journal

SN - 1742-464X

IS - 17

ER -