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char = e;code = 101
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char = p;code = 112
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char = i;code = 105
char = d;code = 100
char = e;code = 101
char = s;code = 115
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char = a;code = 97
char = s;code = 115
char = s;code = 115
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char = t;code = 116
char = h;code = 104
char = e;code = 101
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char = t;code = 116
char = e;code = 101
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char = i;code = 105
char = z;code = 122
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char = o;code = 111
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char = ;code = 32
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char = o;code = 111
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char = o;code = 111
char = s;code = 115
char = y;code = 121
char = s;code = 115
char = t;code = 116
char = e;code = 101
char = m;code = 109
char = ;code = 32
char = I;code = 73
char = I;code = 73
char = .;code = 46
result sql = The action of mercury on the binding of the extrinsic polypeptides associated with the water oxidizing complex of photosystem II.
The action of mercury on the binding of the extrinsic polypeptides associated with the water oxidizing complex of photosystem II.
char = M;code = 77
char = e;code = 101
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char = c;code = 99
char = u;code = 117
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char = H;code = 72
char = g;code = 103
char = 2;code = 50
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char = ,;code = 44
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char = a;code = 97
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char = a;code = 97
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char = -;code = 45
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char = i;code = 105
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char = o;code = 111
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char = o;code = 111
char = s;code = 115
char = y;code = 121
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char = m;code = 109
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char = I;code = 73
char = I;code = 73
char = ;code = 32
char = (;code = 40
char = P;code = 80
char = S;code = 83
char = I;code = 73
char = I;code = 73
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char = .;code = 46
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char = I;code = 73
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char = w;code = 119
char = o;code = 111
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char = k;code = 107
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char = ;code = 32
char = w;code = 119
char = e;code = 101
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char = i;code = 105
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char = e;code = 101
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char = i;code = 105
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char = a;code = 97
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char = e;code = 101
char = d;code = 100
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char = t;code = 116
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char = e;code = 101
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char = i;code = 105
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char = a;code = 97
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char = ;code = 32
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char = e;code = 101
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char = p;code = 112
char = o;code = 111
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char = ;code = 32
char = o;code = 111
char = f;code = 102
char = ;code = 32
char = P;code = 80
char = S;code = 83
char = I;code = 73
char = I;code = 73
char = ;code = 32
char = s;code = 115
char = u;code = 117
char = b;code = 98
char = m;code = 109
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char = m;code = 109
char = b;code = 98
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char = a;code = 97
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char = ;code = 32
char = t;code = 116
char = h;code = 104
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char = e;code = 101
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char = e;code = 101
char = m;code = 109
char = b;code = 98
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char = a;code = 97
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char = i;code = 105
char = n;code = 110
char = ;code = 32
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char = e;code = 101
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char = p;code = 112
char = r;code = 114
char = e;code = 101
char = s;code = 115
char = e;code = 101
char = n;code = 110
char = c;code = 99
char = e;code = 101
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char = f;code = 102
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char = m;code = 109
char = e;code = 101
char = r;code = 114
char = c;code = 99
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char = r;code = 114
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char = p;code = 112
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char = c;code = 99
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char = o;code = 111
char = f;code = 102
char = ;code = 32
char = 3;code = 51
char = 3;code = 51
char = ;code = 32
char = k;code = 107
char = D;code = 68
char = a;code = 97
char = .;code = 46
char = ;code = 32
char = T;code = 84
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char = E;code = 69
char = P;code = 80
char = 3;code = 51
char = 3;code = 51
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char = P;code = 80
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result sql = Mercury (Hg2+), a sulfhydryl group reactant, was used to probe structure-function relationships in photosystem II (PSII). In the present work, we investigated the impact of mercury on the polypeptide composition of PSII submembrane preparations. Electrophoretic analysis revealed that the incubation of the membranes in the presence of mercury produces the depletion of a polypeptide of molecular weight of 33 kDa. This polypeptide corresponds to the extrinsic protein EP33 of the oxygen evolving complex removed following urea treatment. However, the two closely related extrinsic polypeptides of 16 and 23 kDa, usually removed concomitantly after urea treatment, remained unaffected after the mercury treatment. These data demonstrated the existence of an intrinsic binding site for EP23. The molecular mode of action of mercury in the oxygen evolving complex of PSII is discussed.

Publication: FEBS Lett. 1995 Mar 6 ;360(3)::251-4.
Publication Date: 1995 Mar 6
Study Author(s): Bernier, M;Carpentier, R;
Institution: Centre de recherche en photobiophysique, Université du Québec à Trois-Rivières, Canada.
Shortcut link to this study:
Mercury (Hg2+), a sulfhydryl group reactant, was used to probe structure-function relationships in photosystem II (PSII). In the present work, we investigated the impact of mercury on the polypeptide composition of PSII submembrane preparations. Electrophoretic analysis revealed that the incubation of the membranes in the presence of mercury produces the depletion of a polypeptide of molecular weight of 33 kDa. This polypeptide corresponds to the extrinsic protein EP33 of the oxygen evolving complex removed following urea treatment. However, the two closely related extrinsic polypeptides of 16 and 23 kDa, usually removed concomitantly after urea treatment, remained unaffected after the mercury treatment. These data demonstrated the existence of an intrinsic binding site for EP23. The molecular mode of action of mercury in the oxygen evolving complex of PSII is discussed.
PMID: 7883042

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