Abstract

Binuclear and multinuclear manganese containing enzymes which occur in biology are involved in functions such as hydrogen peroxide decomposition in bacteria and the oxidation of water to oxygen during photosynthesis, respectively. In the case of the water-oxidizing complex, the so-called S/sub 2/ oxidation state has been characterized by EPR spectroscopy to be a mixed valence manganese cluster. This can be produced in two forms. The native form, which is found in active O/sub 2/-evolving samples, is considered to be either tetranuclear or trinuclear in Mn, based upon interpretation of its broad 1500 G-wide 19-line multiline EPR signal and unusual temperature dependence. A partially decoupled form is found in inactivated samples having a narrow width (1345 G), with only 16 lines and a more Curie-like temperature dependence, all features which are found in typical Mn/sup 3 +//M/sup 4 +/ binuclear centers (16-line EPR, spin S = 1/2 ground state). For the native form both different oxidation states and different numbers for the manganese ions in the cluster have been proposed in order to account for the larger spectral width due to the hyperfine interaction with /sup 55/Mn. Both binuclear Mn/sup 2 +//Mn/sup 3 +/ and tetranuclear/sup 4/ 3Mn/sup 3 +//Mn/sup 4more » +/ states have been considered. Notably lacking in this analysis has been EPR data for binuclear complexes in which both types of mixed valence oxidation states, Mn/sup 3 +//Mn/sup 4 +/ and Mn/sup 2 +//Mn/sup 3 +/, are compared within the same ligand system. The present report gives the first experimental evidence showing how /sup 55/Mn hyperfine data can easily distinguish between binuclear manganese complexes having these mixed valence oxidation states.« less

Full Text
Published version (Free)

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call