Abstract
Here we examine the classical electron transfer chains of the mitochondrial respiratory oxidoreductase complexes. These chains guide electrons between substrates and energy coupling sites and between the coupling sites themselves. Structural studies on oxidoreductases are showing that several redox cofactors separated in protein by 4–10 Å are often in the form of a chain Long chains are evident in respiratory Complex I, II and in between Complexes III and IV. Calculations show that these chains are able to transfer electrons over very large distances with high directional specificity. Driven by small overall free energies, they operate in the microsecond time scale. Close proximity of the cofactors maintains physiologically productive rates even when substantial thermodynamically unfavorable steps are encountered in the chain. These steps offer potential points of regulation.
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© 1998 Springer Science+Business Media Dordrecht
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Dutton, P.L., Chen, X., Page, C.C., Huang, S., Ohnishi, T., Moser, C.C. (1998). Respiratory Electron Transfer Chains. In: Canters, G.W., Vijgenboom, E. (eds) Biological Electron Transfer Chains: Genetics, Composition and Mode of Operation. NATO ASI Series, vol 512. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-5133-7_1
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DOI: https://doi.org/10.1007/978-94-011-5133-7_1
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