NDLI: The iron–sulfur core in Rieske proteins is not symmetric

Content Provider	Springer Nature Link
Author	Ali, Md. Ehesan Nair, Nisanth N. Retegan, Marius Neese, Frank Staemmler, Volker Marx, Dominik
Copyright Year	2014
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.
Starting Page	1287
Ending Page	1293
Page Count	7
File Format	PDF
ISSN	09498257
Journal	JBIC Journal of Biological Inorganic Chemistry
Volume Number	19
Issue Number	8
e-ISSN	14321327
Language	English
Publisher	Springer Berlin Heidelberg
Publisher Date	2014-08-24
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Iron-sulfur protein Extended broken-symmetry Constraint spin-density dynamics Biochemistry Microbiology
Content Type	Text
Resource Type	Article
Subject	Biochemistry Inorganic Chemistry

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