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Fine Structural Localization of Succinoxidase Complex on the Mitochondrial Cristae

Abstract

SEVERAL methods have been used to demonstrate oxidative enzyme activities in mitochondria, at the electron microscope level. As electron acceptors, potassium tellurite1, and several different tetrazolium salts such as nitro-blue tetrazolium (NBT), tetra nitro-blue tetrazolium chloride (TNBT), thiocarbamyl nitro-blue tetrazolium (TC-NBT), or osmate of tetranitrophenyl stilbene tetrazolium (Os-TNST)2–6, have been used. Recently Ogawa et al.7 introduced a method in which ferricyanide is used as electron acceptor, based on the fact that ferricyanide can accept electrons from the electron transfer chain and the ferrocyanide produced is trapped by copper ions to produce insoluble, electron dense, copper ferrocyanide. It has been shown biochemically8 as well as histochemically7 that the ferricyanide accepts electrons principally at the cytochrome c level. The histochemical reaction therefore demonstrates the greater part of the electron transfer chain.

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KALINA, M., WEAVERS, B. & PEARSE, A. Fine Structural Localization of Succinoxidase Complex on the Mitochondrial Cristae. Nature 221, 479–480 (1969). https://doi.org/10.1038/221479a0

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