Biological systems have evolved active sites containing [4Fe-4S](2+) cluste
rs covalently linked to a mononuclear Fe or Ni or to a diiron cluster. Such
structures have been found in sulfite reductase, carbonmonoxide dehydrogen
ases and most recently in [Fe]-hydrogenases. The link through a bridging li
gand provides an exchange pathway that couples the spins of the two chromop
hores. In this contribution the spin physics of these systems as viewed fro
m a standpoint of Mossbauer spectroscopy is discussed.