Abstract
The investigation of metalloprotein electron transfer mechanisms through structural and functional characterization of modified proteins produced by site-directed mutagenesis provides a systematic means of gaining new, often quantitative, insight into the structural characteristics that regulate the electrochemical, kinetic and protein-binding properties of such proteins. This review discusses aspects of the experimental strategies that have been employed in the application of site-directed mutagenesis as a means of addressing these mechanistic issues, some of the known limitations of this approach, and strategies for expression of recombinant electron transfer proteins. In addition, a detailed summary of the current literature concerning functional studies of engineered mutant forms of cytochrome c is presented to illustrate the manner in which the technique has been employed in studies of this protein as a representative member of this large category of proteins.
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Grant Mauk, A. (1991). Electron transfer in genetically engineered proteins. The cytochrome c paradigm. In: Long-Range Electron Transfer in Biology. Structure and Bonding, vol 75. Springer, Berlin, Heidelberg. https://doi.org/10.1007/3-540-53260-9_5
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DOI: https://doi.org/10.1007/3-540-53260-9_5
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