Abstract
Biological energy conversion in mitochondria is carried out by the membrane protein complexes of the respiratory chain and the mitochondrial ATP synthase in the inner membrane cristae. Recent advances in electron cryomicroscopy have made possible new insights into the structural and functional arrangement of these complexes in the membrane, and how they change with age. This review places these advances in the context of what is already known, and discusses the fundamental questions that remain open but can now be approached.Electronic supplementary materialThe online version of this article (doi:10.1186/s12915-015-0201-x) contains supplementary material, which is available to authorized users.
Highlights
Biological energy conversion in mitochondria is carried out by the membrane protein complexes of the respiratory chain and the mitochondrial adenosine triphosphate (ATP) synthase in the inner membrane cristae
Isolated mitochondria are fully competent for Kühlbrandt BMC Biology (2015) 13:89 respiration and ATP synthesis [11]
We owe much of what we know about mitochondria and how they work at the molecular level to in vitro studies with isolated mitochondria, or even mitochondrial membrane fractions, which still carry out oxidative phosphorylation and ATP synthesis [13]
Summary
Of such differences comes primarily from electron microscopy, because it has not been possible to separate cristae and boundary membranes biochemically. ATP synthase forms rows of dimers in crista membranes The mitochondrial F1-Fo ATP synthase is the most conspicuous protein complex in the cristae. The double rows were thought to be linear arrays of mitochondrial ATP synthase. This is what they are, but it could only be shown unambiguously more than 20 years later by cryo-ET [30, 38], which revealed rows of ATP synthase dimers in mitochondria of all species investigated [30] (Fig. 4). The linear arrays of ATP synthase dimers are a ubiquitous and fundamental attribute of all mitochondria They are always found along the most tightly curved regions along the crista ridges (Additional file 2), or around narrow tubular cristae. Subtomogram averages indicate that dimers from fungi and mammals are indistinguishable at low resolution, whereas those from plants, algae and protists differ in dimer angle or position of the peripheral stalk relative to the catalytic F1
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