Abstract
Biological systems have evolved active sites containing [4Fe-4S]2+ clusters covalently linked to a mononuclear Fe or Ni or to a diiron cluster. Such structures have been found in sulfite reductase, carbonmonoxide dehydrogenases and most recently in [Fe]-hydrogenases. The link through a bridging ligand provides an exchange pathway that couples the spins of the two chromophores. In this contribution the spin physics of these systems as viewed from a standpoint of Mössbauer spectroscopy is discussed.
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Münck, E., Popescu, C.V. Mössbauer studies of exchange coupled cluster assemblies in biological systems. Hyperfine Interactions 126, 59–67 (2000). https://doi.org/10.1023/A:1012632409563
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DOI: https://doi.org/10.1023/A:1012632409563