A ligand-field model to describe a new class of 2Fe-2S clusters in proteins and their synthetic analogues
| Autor: | John F. Gibson, Bruno Guigliarelli, Patrick Bertrand, Beardwood Peter, Jean-Pierre Gayda |
|---|---|
| Rok vydání: | 1985 |
| Předmět: |
chemistry.chemical_classification
Ligand field theory biology Stereochemistry Biophysics Thermus thermophilus biology.organism_classification Biochemistry Spectral line law.invention chemistry Structural Biology law Metalloprotein Rieske protein biology.protein Electron paramagnetic resonance Molecular Biology Ferredoxin |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 831:261-266 |
| ISSN: | 0167-4838 |
| DOI: | 10.1016/0167-4838(85)90044-5 |
| Popis: | Some metalloproteins which contain [2f-2S] clusters give EPR spectra characterized by g av ≈ 1.91, which is significantly lower than the value g av ≈ 1.96 usually obtained for the ferredoxins. A similar lowering of g av is observed for some [2F-2S] + thiolate synthetic compounds in glass-forming solvents, or in compounds where phenolates replace thiolates as terminal ligands. We show that a good correlation is observed for all the proteins and synthetic compounds characterized by g av ≈ 1.91, when the main components, g 1 , g 2 , g 3 , of the g tensor are plotted as a function of ( g 2 − g 3 ). This correlation supports the existence of a new class of [2F-2S] + clusters. A ligand-field analysis shows that the difference between the two kinds of EPR spectrum reflect essentially two different structures for the ferrous site. This conclucsion is in agreement with the spectroscopic studies performed on the Rieske protein from Thermus thermophilus . |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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