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UV-vis spectra showed CO (II) coordination in zinc finger domain of prokaryotic cells

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Document pages: 7 pages

Abstract: The electronic configuration of CO (II) allows it to be used as a spectral probe in UV-Vis spectroscopy experiments to characterize metal coordination spheres as an important part of the functional structure of zinc binding proteins and evaluate the metal ion affinity of these proteins. Here, using the ability of prokaryotic zinc finger and using different residue combinations to properly coordinate structural metal ions, we provided the addition of CO (II) to ros87 and its mutant ros87 The mutant ros87 was characterized by UV-Vis spectrum of c27d C27d has an unusual cysasphish2 coordination ball. Zinc finger sites containing only one cysteine are rarely described. We show a strong D-D transition band of cysasphish2 coordination, which is blue shifted relative to the Cys2His2 sphere. These are dta complemented by NMR and CD data demonstrate that the tetrahedral geometry of the metal site is retained also in the case of a single-cysteine coordination sphere.

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