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The Structure of Cytochrome c Oxidase: Immuno-Electron Microscopy and Image Analysis of Two-Dimensional Crystals

  • Conference paper
Electron Microscopy at Molecular Dimensions

Part of the book series: Proceedings in Life Sciences ((LIFE SCIENCES))

Abstract

Cytochrome c oxidase is the terminal component of mitochondrial electron transport and transfers electrons from reduced cytochrome c to molecular oxygen. Energy from this process is coupled to phosphorylation of ADP to produce ATP, and the mechanism by which electron transport energy is coupled to ATP synthesis involves the generation of an electrochemical gradient of protons across the inner mitochondrial membrane. Cytochrome c oxidase participates in the formation of the proton gradient by consuming protons from the matrix space of the mitochondrion during reduction of molecular oxygen to produce H2O [1]. Wikström and Saari [2] have proposed that cytochrome oxidase also acts as a proton pump and actively transports protons from the matrix side (M-side) to the cytoplasm-facing side (C-side) of the mitochondrial inner membrane.

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© 1980 Springer-Verlag Berlin Heidelberg

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Frey, T.G., Chan, S.H.P. (1980). The Structure of Cytochrome c Oxidase: Immuno-Electron Microscopy and Image Analysis of Two-Dimensional Crystals. In: Baumeister, W., Vogell, W. (eds) Electron Microscopy at Molecular Dimensions. Proceedings in Life Sciences. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-67688-8_10

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  • DOI: https://doi.org/10.1007/978-3-642-67688-8_10

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-67690-1

  • Online ISBN: 978-3-642-67688-8

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