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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Macdonald, G. M. Bixby, K. A. Barry, B. A. |
| Description | Author Affiliation: MacDonald GM ( Department of Biochemistry, University of Minnesota, St. Paul 55108.); |
| Abstract | Photosystem II, the photosynthetic water-oxidizing complex, contains two redox-active tyrosine residues. Although current models suggest that these tyrosines are located in symmetric positions in the reaction center, there are functional differences between them. To elucidate those structural factors that give rise to this functional asymmetry, we have used difference Fourier-transform infrared spectroscopy to obtain the vibrational difference spectrum associated with the oxidation of each of these redox-active residues. Isotopic labeling was employed to definitively assign vibrational lines to the redox-active tyrosines. This work has shown that the vibrational spectra of the two redox-active species are significantly different from each other. This result suggests that the structure of the redox-active residue helps to determine its role in electron transfer in the reaction center. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 23 |
| Volume Number | 90 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 1993-01-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Cyanobacteria Metabolism Photosynthetic Reaction Center Complex Proteins Chemistry Tyrosine Electron Spin Resonance Spectroscopy Manganese Oxidation-Reduction Photosystem II Protein Complex Spectroscopy, Fourier Transform Infrared Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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