The class II cytochromes Rhodospirillum molischianum cytochrome c', Rhodopseudomonas palustris cytochrome C556 and Agrobacterium tumefaciens (B2a) cytochrome c556 have been investigated with a variety of spectroscopic techniques. The cytochrome c' was found to be high-spin and the two cytochromes c556 were found to be mainly low-spin and sx-coordinate with the fifth and sixth ligands being histidine and methionine. The implications of the different types of iron coordination are discussed.