Journal of Inorganic Biochemistry
J04
IRON-SULFUR AND OTHER METAL-SULFUR CLUSTERS
FOLDING/UNFOLDING OF Fe-S PROTEINS
I Bertini, Cowan, J., Luchinat, C., Natarajan, K., Piccioli, M. University of Florence, Department of Chemistry, Via Gino Capponi 7, Florence, 50121, Italy
The 1H NMR spectra of reduced and oxidized High Potential Iron Sulfur Proteins (HiPIP) have led to the resolution of the solution structures (1 - 4) They will be presented and discussed. The full assignment 1H, 13C, 15N allows us to follow the unfolding of the protein with guanidinium chloride. An intermediate is found which is stable only when the protein is in the reduced form (5). These data are interpreted in terms of stability of the protein and of the Fe4S4 cluster. .
2. 3. 4.
Banci. L., Bertini, I., Eltis, L.D., Felli, I.C., Kastrau, D.H.W., Luchinat, C., Piccioli, M., Pierattelli, R., Smith, M., Eur.J.Biochem. 225, 715-725, (1994). Banci, L., Bertini, I., Dikiy, A., Kastrau, D.H.W., Luchinat, C., Sompornpisut, P., Biochemistry 34, 206-219, (1995). Bertini, I., Eltis L.D., Felli, I.C., Kastrau, D.H.W., Luchinat, C., Piccioli, M., Chemistry - A European Journal 1, 598-607, (1995). Bertini, I., Dikiy, A., Kastrau, D.H.W., Luchinat, C., Sompornpisut, P., Biochemistry 34, 9851-9858, (1995). 5) Bertini, I., Cowan, J.A., Luchinat, C., Natarajan, K., Piccioli, M. Submitted.
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