ABSTRACT There are a large number of functionally diverse metalloproteins which contain di- or multi-nuclear metal centers. The metal centers in these metalloproteins can be studied by means of magnetic and spectroscopic techniques using paramagnetic metal ions as intrinsic or external probes. In this review, we discuss the studies of several such metalloproteins by the use of one and two-dimensional nuclear magnetic resonance (NMR) techniques that have been accomplished in the past few years. Three families of such proteins will be discussed in detail: Cu, Zn-superoxide dismutase and its metal-substituted derivatives, dinuclear μ-oxo Fe proteins, and multinuclear hydrolytic Zn enzymes. A brief account is also given on a few other multinuclear metalloproteins that have been investigated with NMR techniques.
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