METALLOPROTEIN - ENDOR- SPECTROSCOPY Structure determination of the prosthetic site from randomly oriented specimen and correlations with NMR-spectroscopy

摘要

The theoretical foundations for the application of high-resolution electron- nuclear-double-resonance spectroscopy to the determination of structural properties of the prosthetic group in randomly oriented metalloproteins are delineated. Applications described involve Superoxide Dismutase as a copper-containing protein and Enoate Reductase as an iron-sulfur protein. Correlations with nuclear magnetic resonance are shown to involve mainly the isotropic coupling for protons as obtained from the paramagnetic shift and the direction of the g-tensor in the molecular framework.