High‐specific binding of Fe(II) at the Mn‐binding site in Mn‐depleted PSII membranes from spinach

Semin, B.K.; Иванов, Ю.Н.; Rubin, A. B.; Parak, F.

doi:10.1016/0014-5793(95)01215-z

Cited by 24 publications

(21 citation statements)

References 19 publications

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“…This explains why we were able to bind two irons to the high-affinity Mn-binding site of Mn-depleted PSII membranes [13). There are additional arguments which suggest that these motifs in the DIID2 heterodimer participate in the coordination of the dinuclear centre of the tetranuclear manganese cluster: (i) mutants which terminate the D2 translation prematurely and mutants which have deletions near the C-domain of D2 have proved the involvement of this region in the formation of the OEC [3); (ii) the replacement of H332 in DI results in the loss of oxygen-evolving activity [25); (iii) the chemical cross-linking analysis has shown that the carboxyl-terminal domains of the DI subunit (D 308 _A334) and those of the D2 subunit (y297_L353) are in close proximity [26); (iv) the Cterminal regions of D I and D2 are highly conserved among the oxygen-evolving species [l9); (v) the Land M subunits of the reaction centres from purple bacteria which do not evolve oxygen have significant homology in the sequence with the DI and D2 polypeptides but a shorter carboxy-terminal extensions [27); (vi) the LFI mutant of Scenedesmus obliquus has no post-translational cleavage of the carboxy-terminal extension of the DI polypeptide and thus a failure to assemble a functional Mn complex [28).…”

Section: Bk Semin F Paraklfebs Letters 400 (1997) 259-262mentioning

confidence: 78%

“…In a preceding work [13] we used Fe (II) and Fe(III) as probes for the high-affinity Mn-binding site of PSII. Using *Corresponding author.…”

Section: Introductionmentioning

confidence: 99%

“…Fe (II) binds to the Mn site in the same way as Mn (II). The following common peculiarities of the interaction of these cations with the Mn-binding site were found: (i) the effective concentration for binding is smaller than I /lM; (ii) the binding is accompanied by the oxidation of the cations; (iii) the affinity of Mn (II) and Fe (II) to this site changes in the presence of different anions in the same manner; (iv) reductants inhibit the binding of Mn (II) and Fe(II) [13]; (v) the ligation of Fe (II) is a light-dependent process leading to the formation of a binuclear 2 Fe(III) cluster, as in the case of Mn(II) [14,15].…”

Section: Introductionmentioning

confidence: 99%

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Coordination sphere and structure of the Mn cluster of the oxygen‐evolving complex in photosynthetic organisms

Semin

Parak

1997

FEBS Letters

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The great similarity between the binding of Fe(II) and the high-affinity Mn-binding site in the Mn-depleted PSII membranes (Semin et al. (1996) FEBS Lett. 375, 223-226) suggests that the coordination sphere of Mn in PSII is also suitable for iron. A comparison is performed between the primary amino acid sequences ofDI and D2 and diiron-oxo enzymes with the function of oxygen activation. All conservative motifs (EXXH) and residues binding and stabilizing the diiron cluster in diiron-oxo enzymes have been found in the C-terminal domains of Dl and D2 polypeptides. On the basis of these sequence similarities we suggest a structural model for the manganese cluster in the oxygen-evolving complex.

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Section: Bk Semin F Paraklfebs Letters 400 (1997) 259-262mentioning

confidence: 78%

“…In a preceding work [13] we used Fe (II) and Fe(III) as probes for the high-affinity Mn-binding site of PSII. Using *Corresponding author.…”

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Coordination sphere and structure of the Mn cluster of the oxygen‐evolving complex in photosynthetic organisms

Semin

Parak

1997

FEBS Letters

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“…In forthcoming studies this material will be used for attempts to reconstitute the 'empty' site with other metal ions. Experiments of this kind were recently successfully performed in PS II membrane fragments deprived of the manganese of the water oxidizing complex ( [37] and references therein).…”

Section: M6ssbauer Measurementsmentioning

confidence: 99%

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

et al. 1996

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“…The incubation of the PSII(-Mn) preparations with Fe(II) ions in the light was also shown to decrease by half the rate of DCIP reduction by the electrons transported from DPC [9]. The inhibition of electron transport from DPC to DCIP by Mn cations as dependent on Fe(II) concentration presumed that Mn and Fe competed for the binding site [10].…”

Section: Introductionmentioning

confidence: 92%

Characteristic features of the interaction between Fe(II) cations and the donor side of the manganese-depleted photosystem II

Lovyagina

Davletshina

Kultysheva

et al. 2005

Russ J Plant Physiol

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Ferrous iron cations Fe(II) can effectively bind to the donor side of the manganese-depleted photosystem II (PSII(-Mn)) and in this way block electron transfer from diphenylcarbazide (DPC) to the major donor for P680, Y Z . The present study was focused on the characteristic features of this process. The oxidation and subsequent binding of Fe(II) cations to PSII(-Mn) may proceed in the absence of an artificial electron acceptor, and therefore we investigated the role of O 2 as a putative endogenous acceptor. Oxygen was shown to participate in the blockade of Y Z by Fe cations, apparently as a structural element of Fe cluster formed at the donor side of PSII(-Mn). The kinetic study of blocking Y Z by Fe(II) as dependent on light intensity demonstrated that the quantum efficiency of Fe cations binding to the donor side of PSII(-Mn) considerably exceeded that of Mn cations. We also compared the possibilities of extracting the native Mn cluster and reconstructed Fe cations from PSII and an alternative electron transport from DPC to P680 + under the conditions of the Y Z blockade by Fe cations. Neither an alternative donor for P680, Y D , nor cytochrome b 559 participated in the latter process. As a whole, our evidence shows that many features of binding Fe cation to the donor side of PSII(-Mn) are in common with photoassembling the Mn cluster.

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High‐specific binding of Fe(II) at the Mn‐binding site in Mn‐depleted PSII membranes from spinach

Cited by 24 publications

References 19 publications

Coordination sphere and structure of the Mn cluster of the oxygen‐evolving complex in photosynthetic organisms

Coordination sphere and structure of the Mn cluster of the oxygen‐evolving complex in photosynthetic organisms

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

Characteristic features of the interaction between Fe(II) cations and the donor side of the manganese-depleted photosystem II

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