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Iron–Sulfur Clusters in Complex I

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A Structural Perspective on Respiratory Complex I

Abstract

Multiple iron-sulfur clusters are found in a variety of metalloproteins such as ferredoxins, hydrogenases, and nitrogenases as well as in complex I (NADH:ubiquinone oxidoreductase) and complex II (succinate:ubiquinone oxidoreductase) of the mitochondrial electron transport chain. Complex I contains two binuclear iron-sulfur clusters, N1a and N1b, and at least six tetranuclear iron-sulfur clusters, N2, N3, N4, N5, N6a, and N6b. An additional cluster N7 is found in some bacteria. The electron transfer pathway in complex I was finally shown in the crystal structure of the hydrophilic portion of Thermus thermophilus complex I. Electrons from NADH are transferred over approximately 95 Å from FMN (flavin mononucleotide) to cluster N2 in the hydrophilic domain of complex I. In addition, the binuclear cluster N1a and the tetranuclear cluster N7 are found not to participate in this pathway. However, not all iron-sulfur clusters have been identified by electron paramagnetic resonance (EPR), which has been the most informative technique for the study of iron-sulfur clusters in complex I for the past four decades. In this chapter, current knowledge on characteristics and roles of each iron-sulfur cluster is overviewed.

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  1. Johnson Research Foundation, Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, 19104, USA

    Eiko Nakamaru-Ogiso

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  1. Eiko Nakamaru-Ogiso
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Correspondence to Eiko Nakamaru-Ogiso .

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  1. , Mitochondrial Biology Unit, Medical Research Council, Hills road, Cambridge, CB2 0XY, Cambridgeshire, United Kingdom

    Leonid Sazanov

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Nakamaru-Ogiso, E. (2012). Iron–Sulfur Clusters in Complex I. In: Sazanov, L. (eds) A Structural Perspective on Respiratory Complex I. Springer, Dordrecht. https://doi.org/10.1007/978-94-007-4138-6_3

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