title: The ribbon structure of the mitochondrial inner membrane.
abstract: Electron microscopic evidence is presented for the extensive association of protein subunits into ribbons within the mitochondrial inner membrane. The mitochondrial cristae can be rearranged to a narrow tubular form which exhibits ribbon structure and is fully functional; the morphology of particles derived from sub-mitochondrial electron transport particles by treatment with lysolecithin suggests that the backbone of the ribbon is provided by the cytochrome-free tripartite unit (headpiece, stalk, basepiece) in linear repeat. These results are inconsistent with any single model of the inner membrane previously proposed, but are best understood in terms of a model which combines the concept of an ordered protein continuum with the concept of a fluid lipid bilayer. Further, it is concluded that the "headpiece out" morphology of the tripartite unit represents a viable conformation of the endergonic transducing unit.
authors.affiliation: Institute for Enzyme Research, University of Wisconsin, Madison, Wisconsin 53706, USA.
authors.forename: R A
authors.initials: RA
authors.lastname: Haworth
authors.forename: H
authors.initials: H
authors.lastname: Komai
authors.forename: D E
authors.initials: DE
authors.lastname: Green
authors.forename: W J
authors.initials: WJ
authors.lastname: Vail
mesh_terms: D000818:Animals; D002417:Cattle; D005614:Freeze Fracturing; D008244:Lysophosphatidylcholines; D008854:Microscopy, Electron; D051336:Mitochondrial Membranes / Q000648:ultrastructure*; D008954:Models, Biological; D009206:Myocardium / Q000166:cytology
chemical_list: D008244:Lysophosphatidylcholines