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Although the NMR chemical shifts and NOEs of the histidine imidazole groups suggest three or four histidine imidazole residues in contact with Zn(II), the NMR data provided little information about the Zn(II) coordination geometry. The NMR structure34 was calculated on the basis of the assumption that the zinc was tetrahedrally coordinated as can be seen in the wild type.49 The visible spectra of the corresponding Co(II) complex and the high catalytic activity of the Zn(II) complex strongly suggest a 6-coordination rather than a 4-coordination for the mutant complex Zn(II)-zf(HHHH). In contrast, the wild complex Zn(II)-zf(CCHH) exactly adopts a tetrahedral geometry through two cysteine and two histidene residues, consistent with the spectral data of the Co(II) complex and no catalytic activity of the Zn(II) complex.
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37
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1542369373
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The d-d bands of Co(II)-zf(HHHH) and the pH dependence of the hydrolytic activity suggest that the zinc center of Zn(II)-zf(HHHH) should adopt a six-coordinate geometry rather than a tetrahedral geometry (Figures 5 and S1), although we have assumed in the previous report that each zinc finger motif of the related three tandem Zn(II)-zf(HHHH) protein has a tetrahedral geometry.34 The three tandem Zn(II)-zf(HHHH) proteins have a high affinity for DNA, despite the structural change of the zinc site from a tetrahedral to a six-coordinate geometry. The three tandem Zn(II)-zf(HHHH) proteins exhibit an α-helix induction upon Zn(II) binding, whose helicity is comparable to the wild type. (The present Zn(II)-zf(HHHH) peptide also induces an α-helix to a similar extent as the wild type.) As well-known, the α-helix region of zinc finger motifs plays a central role in DNA recognition. We think that is the reason the Zn(II)-zf(HHHH) protein retains a high affinity for DNA. The structural change of the zinc center might not significantly decrease the DNA affinity for Zn(II)-zf(HHHH).
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40
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