We have investigated through NMR an extensive series of HiPIPs as well as some ferredoxins in both oxidation states. We have developed a theoretical model for the spin coupling within the cluster that allowed us to rationalize the hyperfine shifts of thecysteine l&and protons as due to the presence of two antierromagnetically coupled spin pairs. The NMR data can thus be interpreted in terms of each individual cysteine beingcoordinated to either an iron belonging to a pair of ferric ions or to a mixed-valence pair.
The electronic structure of Fe4S4 clusters / L., Banci; Battistuzzi, Gianantonio; I., Bertini; Borsari, Marco; F., Capozzi; S., Ciurli; S., Ferretti; C., Luchinat; M., Piccioli; R., Pierattelli; Sola, Marco. - In: JOURNAL OF INORGANIC BIOCHEMISTRY. - ISSN 0162-0134. - STAMPA. - 56:(1994), pp. 52-52. (Intervento presentato al convegno International Workshop on "Iron-Sulfur Proteins: New Structures and Unexpected Functions tenutosi a Konstanz nel 1994).
The electronic structure of Fe4S4 clusters
BATTISTUZZI, Gianantonio;BORSARI, Marco;SOLA, Marco
1994
Abstract
We have investigated through NMR an extensive series of HiPIPs as well as some ferredoxins in both oxidation states. We have developed a theoretical model for the spin coupling within the cluster that allowed us to rationalize the hyperfine shifts of thecysteine l&and protons as due to the presence of two antierromagnetically coupled spin pairs. The NMR data can thus be interpreted in terms of each individual cysteine beingcoordinated to either an iron belonging to a pair of ferric ions or to a mixed-valence pair.
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