Molecular mechanism of action of Pb<sup>2+</sup> and Zn<sup>2+</sup> on water oxidizing complex of photosystem II

Rashid, Abdur; Camm, Edith L.; Ekramoddoullah, A.K.M.

doi:10.1016/0014-5793(94)00789-6

Cited by 64 publications

(31 citation statements)

References 22 publications

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“…In line with many other studies involving independent techniques (Rashid and Popovic, 1990;Berniere et al, 1993;Renger et al, 1993;Rashid et al, 1994;Schroder etal, 1994;Berniere and Carpentier, 1995;Jegerschold et al, 1995), Chi a fluorescence measurements (a lower F v ) show that heavy metal ions inhibit reactions at the donor side of PS II (Murthy etal, 1990;Lidon etal, 1993;Xylander etal, 1996Xylander etal, , 1998and Ouzounidou et al, 1997;Boucher and Carpentier, 1999). Heavy metal ions also inhibit at the acceptor side of PS II (N. Mohanty et al, 1990;Renger et al, 1993 andYruela et al, 1996b).…”

Section: Commonality In Metal Ion Actionsupporting

confidence: 58%

“…B. Bazzaz and Govindjee, 1974b;Poskuta etal, 1987Poskuta etal, ,1988Sgardelis etal, 1994;Moustakas et al, 1994;Poskuta and Waclawczyk-Lach 1995;Poskuta et al, 1996;Lukaszek and Poskuta, 1998;Parys et al, 1998), but stimulates respiration (Poskuta and Wacklawczyk-Lach, 1995;Poskuta et al, 1996;Lukaszek and Poskuta, 1998). The primary site of action of Pb, in intact systems, seems to be the Calvin-Benson cycle (Stiborova et al 1986a,b); photosynthetic electron transport (Rashid et al 1994;Poskuta and Waclawczyk-Lach, 1995;Parys et al, 1998;Romanowska et al, 1998) is less affected. In isolated chloroplasts, Pb interaction with PS I reaction center has been reported, though the PS I showed more tolerance to Pb action than PS II (D. Wong and Govindjee, 1976;Krupa and Baszynski, 1995).…”

Section: G Lead (Pb)mentioning

confidence: 96%

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Chlorophyll a Fluorescence as a Probe of Heavy Metal Ion Toxicity in Plants

Joshi

Mohanty

Chlorophyll a Fluorescence

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Section: Commonality In Metal Ion Actionsupporting

confidence: 58%

Section: G Lead (Pb)mentioning

confidence: 96%

Chlorophyll a Fluorescence as a Probe of Heavy Metal Ion Toxicity in Plants

Joshi

Mohanty

Chlorophyll a Fluorescence

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“…It was reported that a low concentration of Zn 2ϩ (ϳ2 mM) inhibited the activity of PSII and caused dissociation of PsbP and PsbQ from the core complex in spinach PSII (39,40). Presumably, the Zn 2ϩ incorporated into PsbP would hinder proper interaction between the His-144 and Asp-165 residues, and interfere with the function of PsbP.…”

Section: Discussionmentioning

confidence: 99%

The Conserved His-144 in the PsbP Protein Is Important for the Interaction between the PsbP N-terminus and the Cyt b559 Subunit of Photosystem II

Ido

Kakiuchi

Uno

et al. 2012

Journal of Biological Chemistry

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Background:PsbP is an extrinsic subunit of photosystem II in green plants. Results: H144A mutation in PsbP alters the chloride requirement and affects the interaction between its N terminus and the PsbE component of photosystem II. Conclusion:The N-and C-terminal domains of PsbP cooperate to support PSII activity. Significance: This provides important information about the binding characteristics of PsbP in green plant PSII.The PsbP protein regulates the binding properties of Ca 2؉ and Cl ؊ , and stabilizes the Mn cluster of photosystem II (PSII); however, the binding site and topology in PSII have yet to be clarified. Here we report that the structure around His-144 and Asp-165 in PsbP, which is suggested to be a metal binding site, has a crucial role for the functional interaction between PsbP and PSII. The mutated PsbP-H144A protein exhibits reduced ability to retain Cl ؊ anions in PSII, whereas the D165V mutation does not affect PsbP function. Interestingly, H144A/D165V double mutation suppresses the effect of H144A mutation, suggesting that these residues have a role other than metal binding. FTIR difference spectroscopy suggests that H144A/D165V restores proper interaction with PSII and induces the conformational change around the Mn cluster during the S 1 /S 2 transition. Cross-linking experiments show that the H144A mutation affects the direct interaction between PsbP and the Cyt b 559 ␣ subunit of PSII (the PsbE protein). However, this interaction is restored in the H144A/D165V mutant. In the PsbP structure, His-144 and Asp-165 form a salt bridge. H144A mutation is likely to disrupt this bridge and liberate Asp-165, inhibiting the proper PsbP-PSII interaction. Finally, mass spectrometric analysis has identified the cross-linked sites of PsbP and PsbE as Ala-1 and Glu-57, respectively. Therefore His-144, in the C-terminal domain of PsbP, plays a crucial role in maintaining proper N terminus interaction. These data provide important information about the binding characteristics of PsbP in green plant PSII.Photosystem II (PSII) 2 consists of both membrane-intrinsic and membrane-extrinsic subunits, and functions as a water/ plastoquinone oxidoreductase (for reviews, Refs. 1-4). On the thylakoid lumenal side of PSII, a metal cluster of four Mn ions, one Ca 2ϩ ion, and five oxo ligands (the Mn cluster) catalyzes the oxygen-evolving reaction. Additionally, two Cl Ϫ ions are bound near to the Mn cluster (5). The membrane-intrinsic subunits of PSII are involved in pigment and/or cofactor binding for photochemical reactions, while the membrane-extrinsic subunits surround the catalytic Mn cluster and play crucial roles in stabilizing the Mn cluster and retaining the PSII cofactor ions (6 -8).X-ray structural analysis of the cyanobacterial PSII complex at atomic resolution has revealed the location of subunits, pigments, and cofactors, including the exact organization of the subunits within PSII (5, 9 -11). However, the crystallographic information gained from the study of cyanobacterial PSII cannot necessarily be...

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“…It is well documented that lead has an inhibitory effect on the donor site of PS 2 (Becerill et al 1988, Rashid and Popovic 1990, Rashid et al 1994 and the degree of coupling in the electron transport chain decreases in response to the heavy metal treatment (Lucerno et al 1976. Mitochondria are known to be much more resistant to heavy metals than chloroplasts as they remain undisturbed even at high metal concentration (Ernst 1998.…”

Section: Introductionmentioning

confidence: 97%

Effect of Pb ions on superoxide dismutase and catalase activities in leaves of pea plants grown in high and low irradiance

Romanowska¹,

Wróblewska²,

Drożak³

et al. 2008

Biol. plant.

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The role of irradiance on the activity of antioxidant enzymes: superoxide dismutase (SOD) and catalase (CAT) was examined in the leaves of Pisum sativum L. plants grown under low (LL) or high (HL) irradiance (PPFD 50 or 600 μmol m -2 s -1 ) and exposed after detachment to 5 mM Pb (NO 3 ) 2 for 24 h. The activities of both enzymes increased in response to LL compared with HL and no effect of Pb ions was observed. Photosystem (PS) 1 and PS 2 activities were also investigated in chloroplasts isolated from these leaves. LL lowered PS 1 electron transport rate and changes in photochemical activity of PS 1 induced by Pb 2+ were visible only in the chloroplasts isolated from leaves of LL grown plants. PS 2 activity was influenced similarly by Pb ions at both PPFD. This study demonstrates that leaves of HL grown plants were less sensitive to lead toxicity than those from LL grown plants. Changes in electron transport rates were the main factors responsible for the generation of reactive oxygen species in the chloroplasts and as a consequence, in induction of antioxidant enzymes.Additional key words: antioxidative enzymes, chloroplasts, lead, Pisum sativum, photosystem 1 and 2 activities.

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Molecular mechanism of action of Pb²⁺ and Zn²⁺ on water oxidizing complex of photosystem II

Cited by 64 publications

References 22 publications

Chlorophyll a Fluorescence as a Probe of Heavy Metal Ion Toxicity in Plants

Chlorophyll a Fluorescence as a Probe of Heavy Metal Ion Toxicity in Plants

The Conserved His-144 in the PsbP Protein Is Important for the Interaction between the PsbP N-terminus and the Cyt b559 Subunit of Photosystem II

Effect of Pb ions on superoxide dismutase and catalase activities in leaves of pea plants grown in high and low irradiance

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Molecular mechanism of action of Pb2+ and Zn2+ on water oxidizing complex of photosystem II

Cited by 64 publications

References 22 publications

Chlorophyll a Fluorescence as a Probe of Heavy Metal Ion Toxicity in Plants

Chlorophyll a Fluorescence as a Probe of Heavy Metal Ion Toxicity in Plants

The Conserved His-144 in the PsbP Protein Is Important for the Interaction between the PsbP N-terminus and the Cyt b559 Subunit of Photosystem II

Effect of Pb ions on superoxide dismutase and catalase activities in leaves of pea plants grown in high and low irradiance

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Molecular mechanism of action of Pb²⁺ and Zn²⁺ on water oxidizing complex of photosystem II