It has been shown that EPR observations of a polynuclear Mn cluster in spinach chloroplasts can be interpreted in terms of a cluster containing three Mn(III) ions and one Mn(IV) ion within a tetranuclear complex. Both ferromagnetic and antiferromagnetic interactions appear to exist between the Mn ions, which exhibit deeply trapped discrete oxidation states, at least in this EPR active state. These results are discussed in terms of what is currently known about the polypeptide composition of the enzyme. A model of the oxidation state changes in the enzyme is proposed which is consistent with the EPR and protein isolation studies. Finally, a comparison between the electron-transporting metalloenzymes and the electron-storing metalloenzymes shows that the facile electron transfer kinetics observed in the former class and the slow kinetics observed in the latter class are consistent with the distinctly different electronic structures of these enzymes and their functional roles.