Iron-Sulfur Proteins: An Insight into their Electronic Structure Through 1H NMR Spectroscopy

摘要: 1H NMR studies of electron transport proteins containing Fe—S polynuclear centers have revealed to be fundamental importance for the understanding electronic and molecular structure such systems. nuclear Overhauser effects saturation transfer experiments allowed us perform assignments β —CH2 cysteines directly coordinated in reduced oxidized states. Such made possible extract from parameters their temperature dependence specific information on magnetic interactions within metal centers. We extended theoretical approach, pioneered by Palmer [1,2] dinuclear Girerd, Munck et al. [3,4] Fe3S4 complexes order account details spectra Fe2S2 Fe4S4 This allows a complete rationalization data including occurrence signals with anti—Curie behavior presence upfield shifts. Further implications are analyzed discussed.