A high potential acceptor for Photosystem II

Bowes, Jane M.; Crofts, Antony R.; Itoh, Shigeru

doi:10.1016/0005-2728(79)90014-8

Cited by 83 publications

(51 citation statements)

References 21 publications

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“…2 = -~-480 mV. This value is somewhat higher than recent data obtained with PSII preparations from Chlamydomonas reinhardtii mutants (Petrouleas and Diner 1986) and spinach thylakoids (Bowes et al 1979). The slight variation of the Em-value could be due to small differences in the microenvironment at the PSII acceptor side caused by Triton X 100 treatment as discussed recently ).…”

Section: Flash-induced Protolytic Reactions In Dark-adapted Psii Membmentioning

confidence: 55%

Studies on the protolytic reactions coupled with water cleavage in photosystem II membrane fragments from spinach

Ренгер¹,

Wacker²,

Völker³

1987

Photosynth Res

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The protolytic reactions of PSII membrane fragments were analyzed by measurements of absorption changes of the water soluble indicator dye bromocresol purple induced by a train of 10 μs flashes in dark-adapted samples. It was found that: a) in the first flash a rapid H(+)-release takes place followed by a slower H(+)-uptake. The deprotonation is insensitive to DCMU but is completely eliminated by linolenic acid treatment of the samples; b) the extent of the H(+)-uptake in the first flash depends on the redox potential of the suspension. In this time domain no H(+)-uptake is observed in the subsequent flashes; c) the extent of the H(+)-release as a function of the flash number in the sequence exhibits a characteristic oscillation pattern. Multiphasic release kinetics are observed. The oscillation pattern can be satisfactorily described by a 1, 0, 1, 2 stoichiometry for the redox transitions Si → Si+1 (i=0, 1, 2, 3) in the water oxidizing enzyme system Y. The H(+)-uptake after the first flash is assumed to be a consequence of the very fast reduction of oxidized Q400(Fe(3+)) formed due to dark incubation with K3[Fe(CN)6]. The possible participation of component Z in the deprotonation reactions at the PSII donor side is discussed.

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Section: Flash-induced Protolytic Reactions In Dark-adapted Psii Membmentioning

confidence: 55%

Studies on the protolytic reactions coupled with water cleavage in photosystem II membrane fragments from spinach

Ренгер¹,

Wacker²,

Völker³

1987

Photosynth Res

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“…These effects are clearly related to the redox state of QB. Another redox active component of functional relevance for the PS II acceptor side is C-400 that becomes oxidized by K3[Fe(CN)G] at sufficiently high redox potentials [29,30]. Recently evidence has been presented for the identification of C-400 with the high-spin Fe2+ [31] that is associated with QA and Qn [32,33].…”

Section: Resultsmentioning

confidence: 99%

The susceptibility of the P‐benzoquinone‐mediated electron transport and atrazine binding to trypsin and its modification by CaCl₂ in thylakoids and PS II membrane fragments

Ренгер¹,

Hagemann²,

Fromme³

1986

FEBS Letters

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Comparative studies in thylakoids and oxygen-evolving Triton X-100 PS II membrane fragments reveal: (i) There exists one high-affinity atrazine binding site per PS II in both preparations. The affinity is reduced in PS II membrane fragments. (ii) The susceptibility to tryptic attack on atrazine binding and p-BQ-mediated electron transport is markedly reduced by CaC12 in PS II membrane fragments, but no protection is observed in thylakoids. NH20H and Ks[Fe(CN),] both reduce the binding affinity in PS II membrane fragments. The action of NH20H is invariant to CaC12 addition. The implications of these findings for functional studies with PS II membrane fragments are discussed. Photosystem II membrane fragment A trazine binding Trypsin effect CaCIJprotection Hydroxylamine effectPotassium ferricyanide effect

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“…The ligation of Fe 2+ by four histidines is assumed to be similar in both types of organisms (two from each of the L and M subunits of the heterodimer forming the reaction center apoprotein of purple bacteria and of the DI and D2 polypeptide of PS II) [5][6][7] while the glutamate ligand in the former type is probably replaced by bicarbonate in PS II [8]. Differences also exist with respect to the redox potential that is significantly lower in PS II for the couple Fe2+/Fe 3+ [9][10][11].…”

Section: Introductionmentioning

confidence: 99%

Isolation and properties of PS II membrane fragments depleted of the non heme iron center

et al. 1996

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A high potential acceptor for Photosystem II

Cited by 83 publications

References 21 publications

Studies on the protolytic reactions coupled with water cleavage in photosystem II membrane fragments from spinach

Studies on the protolytic reactions coupled with water cleavage in photosystem II membrane fragments from spinach

The susceptibility of the P‐benzoquinone‐mediated electron transport and atrazine binding to trypsin and its modification by CaCl₂ in thylakoids and PS II membrane fragments

Isolation and properties of PS II membrane fragments depleted of the non heme iron center

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A high potential acceptor for Photosystem II

Cited by 83 publications

References 21 publications

Studies on the protolytic reactions coupled with water cleavage in photosystem II membrane fragments from spinach

Studies on the protolytic reactions coupled with water cleavage in photosystem II membrane fragments from spinach

The susceptibility of the P‐benzoquinone‐mediated electron transport and atrazine binding to trypsin and its modification by CaCl2 in thylakoids and PS II membrane fragments

Isolation and properties of PS II membrane fragments depleted of the non heme iron center

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The susceptibility of the P‐benzoquinone‐mediated electron transport and atrazine binding to trypsin and its modification by CaCl₂ in thylakoids and PS II membrane fragments