Electron transfer from Cyt b 559 and tyrosine-D to the S 2 and S3 states of the water oxidizing complex in photosystem II at cryogenic temperatures

Yashar Feyziyev, Z. Deák, Stenbjörn Styring, Gábor Bernát

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

The Mn4CaO5 cluster of photosystem II (PSII) catalyzes the oxidation of water to molecular oxygen through the light-driven redox S-cycle. The water oxidizing complex (WOC) forms a triad with TyrosineZ and P680, which mediates electrons from water towards the acceptor side of PSII. Under certain conditions two other redox-active components, TyrosineD (YD) and Cytochrome b 559 (Cyt b 559) can also interact with the S-states. In the present work we investigate the electron transfer from Cyt b 559 and YD to the S2 and S3 states at 195 K. First, YD and Cyt b 559 were chemically reduced. The S2 and S3 states were then achieved by application of one or two laser flashes, respectively, on samples stabilized in the S1 state. EPR signals of the WOC (the S2-state multiline signal, ML-S2), YD and oxidized Cyt b 559 were simultaneously detected during a prolonged dark incubation at 195 K. During 163 days of incubation a large fraction of the S2 population decayed to S1 in the S2 samples by following a single exponential decay. Differently, S3 samples showed an initial increase in the ML-S2 intensity (due to S 3 to S2 conversion) and a subsequent slow decay due to S2 to S1 conversion. In both cases, only a minor oxidation of YD was observed. In contrast, the signal intensity of the oxidized Cyt b 559 showed a two-fold increase in both the S 2 and S3 samples. The electron donation from Cyt b 559 was much more efficient to the S2 state than to the S3 state.

Original languageEnglish
Pages (from-to)111-120
Number of pages10
JournalJournal of Bioenergetics and Biomembranes
Volume45
Issue number1-2
DOIs
Publication statusPublished - Feb 2013

Fingerprint

Photosystem II Protein Complex
Tyrosine
Electrons
Temperature
Water
Oxidation-Reduction
cytochrome b559
Lasers
Oxygen
Light
Population

Keywords

  • Cytochrome b
  • EPR
  • Photosystem II
  • S-states
  • Tyrosine radical
  • Water oxidation

ASJC Scopus subject areas

  • Physiology
  • Cell Biology

Cite this

Electron transfer from Cyt b 559 and tyrosine-D to the S 2 and S3 states of the water oxidizing complex in photosystem II at cryogenic temperatures. / Feyziyev, Yashar; Deák, Z.; Styring, Stenbjörn; Bernát, Gábor.

In: Journal of Bioenergetics and Biomembranes, Vol. 45, No. 1-2, 02.2013, p. 111-120.

Research output: Contribution to journalArticle

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abstract = "The Mn4CaO5 cluster of photosystem II (PSII) catalyzes the oxidation of water to molecular oxygen through the light-driven redox S-cycle. The water oxidizing complex (WOC) forms a triad with TyrosineZ and P680, which mediates electrons from water towards the acceptor side of PSII. Under certain conditions two other redox-active components, TyrosineD (YD) and Cytochrome b 559 (Cyt b 559) can also interact with the S-states. In the present work we investigate the electron transfer from Cyt b 559 and YD to the S2 and S3 states at 195 K. First, YD • and Cyt b 559 were chemically reduced. The S2 and S3 states were then achieved by application of one or two laser flashes, respectively, on samples stabilized in the S1 state. EPR signals of the WOC (the S2-state multiline signal, ML-S2), YD • and oxidized Cyt b 559 were simultaneously detected during a prolonged dark incubation at 195 K. During 163 days of incubation a large fraction of the S2 population decayed to S1 in the S2 samples by following a single exponential decay. Differently, S3 samples showed an initial increase in the ML-S2 intensity (due to S 3 to S2 conversion) and a subsequent slow decay due to S2 to S1 conversion. In both cases, only a minor oxidation of YD was observed. In contrast, the signal intensity of the oxidized Cyt b 559 showed a two-fold increase in both the S 2 and S3 samples. The electron donation from Cyt b 559 was much more efficient to the S2 state than to the S3 state.",
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T1 - Electron transfer from Cyt b 559 and tyrosine-D to the S 2 and S3 states of the water oxidizing complex in photosystem II at cryogenic temperatures

AU - Feyziyev, Yashar

AU - Deák, Z.

AU - Styring, Stenbjörn

AU - Bernát, Gábor

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N2 - The Mn4CaO5 cluster of photosystem II (PSII) catalyzes the oxidation of water to molecular oxygen through the light-driven redox S-cycle. The water oxidizing complex (WOC) forms a triad with TyrosineZ and P680, which mediates electrons from water towards the acceptor side of PSII. Under certain conditions two other redox-active components, TyrosineD (YD) and Cytochrome b 559 (Cyt b 559) can also interact with the S-states. In the present work we investigate the electron transfer from Cyt b 559 and YD to the S2 and S3 states at 195 K. First, YD • and Cyt b 559 were chemically reduced. The S2 and S3 states were then achieved by application of one or two laser flashes, respectively, on samples stabilized in the S1 state. EPR signals of the WOC (the S2-state multiline signal, ML-S2), YD • and oxidized Cyt b 559 were simultaneously detected during a prolonged dark incubation at 195 K. During 163 days of incubation a large fraction of the S2 population decayed to S1 in the S2 samples by following a single exponential decay. Differently, S3 samples showed an initial increase in the ML-S2 intensity (due to S 3 to S2 conversion) and a subsequent slow decay due to S2 to S1 conversion. In both cases, only a minor oxidation of YD was observed. In contrast, the signal intensity of the oxidized Cyt b 559 showed a two-fold increase in both the S 2 and S3 samples. The electron donation from Cyt b 559 was much more efficient to the S2 state than to the S3 state.

AB - The Mn4CaO5 cluster of photosystem II (PSII) catalyzes the oxidation of water to molecular oxygen through the light-driven redox S-cycle. The water oxidizing complex (WOC) forms a triad with TyrosineZ and P680, which mediates electrons from water towards the acceptor side of PSII. Under certain conditions two other redox-active components, TyrosineD (YD) and Cytochrome b 559 (Cyt b 559) can also interact with the S-states. In the present work we investigate the electron transfer from Cyt b 559 and YD to the S2 and S3 states at 195 K. First, YD • and Cyt b 559 were chemically reduced. The S2 and S3 states were then achieved by application of one or two laser flashes, respectively, on samples stabilized in the S1 state. EPR signals of the WOC (the S2-state multiline signal, ML-S2), YD • and oxidized Cyt b 559 were simultaneously detected during a prolonged dark incubation at 195 K. During 163 days of incubation a large fraction of the S2 population decayed to S1 in the S2 samples by following a single exponential decay. Differently, S3 samples showed an initial increase in the ML-S2 intensity (due to S 3 to S2 conversion) and a subsequent slow decay due to S2 to S1 conversion. In both cases, only a minor oxidation of YD was observed. In contrast, the signal intensity of the oxidized Cyt b 559 showed a two-fold increase in both the S 2 and S3 samples. The electron donation from Cyt b 559 was much more efficient to the S2 state than to the S3 state.

KW - Cytochrome b

KW - EPR

KW - Photosystem II

KW - S-states

KW - Tyrosine radical

KW - Water oxidation

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