Abstract
The iron proteins as a general group of biological materials, due to their crucial biological functions and their varied physical characteristics, have been of considerable interest to the biologist and physicist alike. The importance of iron in biological systems lies in its versatility as a trace metal element. The relative ease with which iron can be reduced and oxidized makes it an excellent candidate for the active sites of proteins and enzymes that participate in electron transfer processes. Moreover, it can bind and orient molecules that react while bound to it, and it can also exist as Fe2+, Fe3+, and sometimes as Fe4+ in a variety of crystalline fields in high or low spin configurations.(1) The present study is concerned with the means through which living organisms obtain and secure iron, namely the iron storage and transport proteins.
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Supported in part by the National Science Foundation, PHS Grant AM 15725-01 and the Office of Naval Research.
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Spartalian, K., Oosterhuis, W.T., Window, B. (1973). Mössbauer Effect Studies of Iron Storage and Transport Proteins. In: Gruverman, I.J., Seidel, C.W. (eds) Mössbauer Effect Methodology. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-3162-9_9
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DOI: https://doi.org/10.1007/978-1-4684-3162-9_9
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