1H NMR studies of Cr(NH3)6 3+ binding to spinach plastocyanin
All the aromatic and most of the methyl group resonances in the 1H NMR spectrum of Cu(I) spinach plastocyanin have been assigned. The binding of the paramagnetic cation Cr(NH3)63+ to the protein has been investigated by both one- and two-dimensional NMR techniques. This relaxation probe causes the b...
| Main Authors: | , , , |
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| Format: | Journal article |
| Language: | English |
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1986
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| _version_ | 1797064898952298496 |
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| author | Armstrong, F Driscoll, P Hill, H Redfield, C |
| author_facet | Armstrong, F Driscoll, P Hill, H Redfield, C |
| author_sort | Armstrong, F |
| collection | OXFORD |
| description | All the aromatic and most of the methyl group resonances in the 1H NMR spectrum of Cu(I) spinach plastocyanin have been assigned. The binding of the paramagnetic cation Cr(NH3)63+ to the protein has been investigated by both one- and two-dimensional NMR techniques. This relaxation probe causes the broadening of several resonances in the aliphatic region of the spectrum corresponding to spatially separated groups, thus reflecting a large Cr(NH3)63+ -accessible surface. Three groups of negatively charged residues are tentatively assigned as cation binding "sites" on the protein surface. © 1986. |
| first_indexed | 2024-03-06T21:20:54Z |
| format | Journal article |
| id | oxford-uuid:41690d41-d9e8-4ec4-b658-f293f721577c |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T21:20:54Z |
| publishDate | 1986 |
| record_format | dspace |
| spelling | oxford-uuid:41690d41-d9e8-4ec4-b658-f293f721577c2022-03-26T14:43:31Z 1H NMR studies of Cr(NH3)6 3+ binding to spinach plastocyaninJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:41690d41-d9e8-4ec4-b658-f293f721577cEnglishSymplectic Elements at Oxford1986Armstrong, FDriscoll, PHill, HRedfield, CAll the aromatic and most of the methyl group resonances in the 1H NMR spectrum of Cu(I) spinach plastocyanin have been assigned. The binding of the paramagnetic cation Cr(NH3)63+ to the protein has been investigated by both one- and two-dimensional NMR techniques. This relaxation probe causes the broadening of several resonances in the aliphatic region of the spectrum corresponding to spatially separated groups, thus reflecting a large Cr(NH3)63+ -accessible surface. Three groups of negatively charged residues are tentatively assigned as cation binding "sites" on the protein surface. © 1986. |
| spellingShingle | Armstrong, F Driscoll, P Hill, H Redfield, C 1H NMR studies of Cr(NH3)6 3+ binding to spinach plastocyanin |
| title |
1H NMR studies of Cr(NH3)6
3+ binding to spinach plastocyanin |
| title_full |
1H NMR studies of Cr(NH3)6
3+ binding to spinach plastocyanin |
| title_fullStr |
1H NMR studies of Cr(NH3)6
3+ binding to spinach plastocyanin |
| title_full_unstemmed |
1H NMR studies of Cr(NH3)6
3+ binding to spinach plastocyanin |
| title_short |
1H NMR studies of Cr(NH3)6
3+ binding to spinach plastocyanin |
| title_sort | 1h nmr studies of cr nh3 6 3 binding to spinach plastocyanin |
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