Abstract
Metal complexes are at the heart of many biological processes. Remarkably few structural motifs are used by Nature to accomplish such diverse functions as oxidation and reduction, hydrolysis and condensation, transport of electrons and small molecules, and transformations of chemical energy into electrical and mechanical energy. One of the challenges of bioinorganic chemistry is to relate, for a particular structural motif such as a heme group, the structural features of not only the metal center but also the surroundings to the function and reactivity of the metalloprotein. While much effort has been devoted to relating the stereochemistry of the active site of metalloproteins to thermodynamic aspects of function, there is increasing interest in the stereochemical basis of kinetic aspects of protein function, such as rates of electron transfer, rates of ligand binding and reaction mechanisms for enzymes.
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Jameson, G.B. (1990). Model Systems and Structure, Function and Reactivity Relationships in Transition Metal-Containing Biopolymers. In: Pittman, C.U., Carraher, C.E., Zeldin, M., Sheats, J.E., Culbertson, B.M. (eds) Metal-Containing Polymeric Materials. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-0669-6_35
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