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The iron–sulfur core in Rieske proteins is not symmetric

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Retegan,  Marius
Research Department Neese, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

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Neese,  Frank
Research Department Neese, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

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Citation

Ali, M. E., Nair, N. N., Retegan, M., Neese, F., Staemmler, V., & Marx, D. (2014). The iron–sulfur core in Rieske proteins is not symmetric. Journal of Biological Inorganic Chemistry, 19(8), 1287-1293. doi:10.1007/s00775-014-1185-7.


Cite as: http://hdl.handle.net/21.11116/0000-0007-A82E-9
Abstract
At variance with ferredoxins, Rieske-type proteins contain a chemically asymmetric iron–sulfur cluster. Nevertheless, X-ray crystallography apparently finds their [2Fe–2S] cores to be structurally symmetric or very close to symmetric (i.e. the four iron–sulfur bonds in the [2Fe–2S] core are equidistant). Using a combination of advanced density-based approaches, including finite-temperature molecular dynamics to access thermal fluctuations and free-energy profiles, in conjunction with correlated wavefunction-based methods we clearly predict an asymmetric core structure. This reveals a fundamental and intrinsic difference within the iron–sulfur clusters hosted by Rieske proteins and ferredoxins and thus opens up a new dimension for the ongoing efforts in understanding the role of Rieske-type [2Fe–2S] cluster in electron transfer processes that occur in almost all biological systems.