Co(II) Coordination in Prokaryotic Zinc Finger Domains as Revealed by UV-Vis Spectroscopy
Co(II) electronic configuration allows its use as a spectroscopic probe in UV-Vis experiments to characterize the metal coordination sphere that is an essential component of the functional structure of zinc-binding proteins and to evaluate the metal ion affinities of these proteins. Here, exploiting...
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| Format: | Article |
| Language: | English |
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Wiley
2017-01-01
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| Series: | Bioinorganic Chemistry and Applications |
| Online Access: | http://dx.doi.org/10.1155/2017/1527247 |
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| author | Valeria Sivo Gianluca D’Abrosca Luigi Russo Rosa Iacovino Paolo Vincenzo Pedone Roberto Fattorusso Carla Isernia Gaetano Malgieri |
| author_facet | Valeria Sivo Gianluca D’Abrosca Luigi Russo Rosa Iacovino Paolo Vincenzo Pedone Roberto Fattorusso Carla Isernia Gaetano Malgieri |
| author_sort | Valeria Sivo |
| collection | DOAJ |
| description | Co(II) electronic configuration allows its use as a spectroscopic probe in UV-Vis experiments to characterize the metal coordination sphere that is an essential component of the functional structure of zinc-binding proteins and to evaluate the metal ion affinities of these proteins. Here, exploiting the capability of the prokaryotic zinc finger to use different combinations of residues to properly coordinate the structural metal ion, we provide the UV-Vis characterization of Co(II) addition to Ros87 and its mutant Ros87_C27D which bears an unusual CysAspHis2 coordination sphere. Zinc finger sites containing only one cysteine have been infrequently characterized. We show for the CysAspHis2 coordination an intense d-d transition band, blue-shifted with respect to the Cys2His2 sphere. These data 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. |
| format | Article |
| id | doaj-art-2c249b1faaf646809530fea1b994999f |
| institution | Kabale University |
| issn | 1565-3633 1687-479X |
| language | English |
| publishDate | 2017-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | Bioinorganic Chemistry and Applications |
| spelling | doaj-art-2c249b1faaf646809530fea1b994999f2025-02-03T07:26:11ZengWileyBioinorganic Chemistry and Applications1565-36331687-479X2017-01-01201710.1155/2017/15272471527247Co(II) Coordination in Prokaryotic Zinc Finger Domains as Revealed by UV-Vis SpectroscopyValeria Sivo0Gianluca D’Abrosca1Luigi Russo2Rosa Iacovino3Paolo Vincenzo Pedone4Roberto Fattorusso5Carla Isernia6Gaetano Malgieri7Department of Environmental, Biological and Pharmaceutical Science and Technology, University of Campania-Luigi Vanvitelli, Via Vivaldi 43, 81100 Caserta, ItalyDepartment of Environmental, Biological and Pharmaceutical Science and Technology, University of Campania-Luigi Vanvitelli, Via Vivaldi 43, 81100 Caserta, ItalyDepartment of Environmental, Biological and Pharmaceutical Science and Technology, University of Campania-Luigi Vanvitelli, Via Vivaldi 43, 81100 Caserta, ItalyDepartment of Environmental, Biological and Pharmaceutical Science and Technology, University of Campania-Luigi Vanvitelli, Via Vivaldi 43, 81100 Caserta, ItalyDepartment of Environmental, Biological and Pharmaceutical Science and Technology, University of Campania-Luigi Vanvitelli, Via Vivaldi 43, 81100 Caserta, ItalyDepartment of Environmental, Biological and Pharmaceutical Science and Technology, University of Campania-Luigi Vanvitelli, Via Vivaldi 43, 81100 Caserta, ItalyDepartment of Environmental, Biological and Pharmaceutical Science and Technology, University of Campania-Luigi Vanvitelli, Via Vivaldi 43, 81100 Caserta, ItalyDepartment of Environmental, Biological and Pharmaceutical Science and Technology, University of Campania-Luigi Vanvitelli, Via Vivaldi 43, 81100 Caserta, ItalyCo(II) electronic configuration allows its use as a spectroscopic probe in UV-Vis experiments to characterize the metal coordination sphere that is an essential component of the functional structure of zinc-binding proteins and to evaluate the metal ion affinities of these proteins. Here, exploiting the capability of the prokaryotic zinc finger to use different combinations of residues to properly coordinate the structural metal ion, we provide the UV-Vis characterization of Co(II) addition to Ros87 and its mutant Ros87_C27D which bears an unusual CysAspHis2 coordination sphere. Zinc finger sites containing only one cysteine have been infrequently characterized. We show for the CysAspHis2 coordination an intense d-d transition band, blue-shifted with respect to the Cys2His2 sphere. These data 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.http://dx.doi.org/10.1155/2017/1527247 |
| spellingShingle | Valeria Sivo Gianluca D’Abrosca Luigi Russo Rosa Iacovino Paolo Vincenzo Pedone Roberto Fattorusso Carla Isernia Gaetano Malgieri Co(II) Coordination in Prokaryotic Zinc Finger Domains as Revealed by UV-Vis Spectroscopy Bioinorganic Chemistry and Applications |
| title | Co(II) Coordination in Prokaryotic Zinc Finger Domains as Revealed by UV-Vis Spectroscopy |
| title_full | Co(II) Coordination in Prokaryotic Zinc Finger Domains as Revealed by UV-Vis Spectroscopy |
| title_fullStr | Co(II) Coordination in Prokaryotic Zinc Finger Domains as Revealed by UV-Vis Spectroscopy |
| title_full_unstemmed | Co(II) Coordination in Prokaryotic Zinc Finger Domains as Revealed by UV-Vis Spectroscopy |
| title_short | Co(II) Coordination in Prokaryotic Zinc Finger Domains as Revealed by UV-Vis Spectroscopy |
| title_sort | co ii coordination in prokaryotic zinc finger domains as revealed by uv vis spectroscopy |
| url | http://dx.doi.org/10.1155/2017/1527247 |
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