Differential shifts for the backbone nuclei in the two oxidation states of Chromatium vinosum HiPIP are observed. The sizable differential shifts close to the [Fe 4S 4] n+ cluster are accounted for by the different paramagnetic effects. Residual effects, largest for peptide nitrogens and not due to known paramagnetic effects, are present at large distances. They arise from the charge difference between the two redox forms of the protein through either long-range conformational changes, polarization effects, or both.
Redox related chemical shift perturbations on backbone nuclei of high-potential iron sulfur proteins / LUCHINAT C; LEHMANN T; M. PICCIOLI. - In: INORGANIC CHEMISTRY. - ISSN 0020-1669. - STAMPA. - 41:(2002), pp. 1679-1683. [10.1021/ic010761i]
Redox related chemical shift perturbations on backbone nuclei of high-potential iron sulfur proteins
LUCHINAT, CLAUDIO;PICCIOLI, MARIO
2002
Abstract
Differential shifts for the backbone nuclei in the two oxidation states of Chromatium vinosum HiPIP are observed. The sizable differential shifts close to the [Fe 4S 4] n+ cluster are accounted for by the different paramagnetic effects. Residual effects, largest for peptide nitrogens and not due to known paramagnetic effects, are present at large distances. They arise from the charge difference between the two redox forms of the protein through either long-range conformational changes, polarization effects, or both.
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