Work

Scanning transmission electron microscopic study of alpha-ketoglutarate dehydrogenase complex from Escherichia coli.

Year: 1987

Type: article

Abstract: The alpha-ketoglutarate dehydrogenase complex was resolved into its three component enzymes: alpha-ketoglutarate dehydrogenase (E1), dihydrolipoyl transsuccinylase (E2), and dihydrolipoyl dehydrogenase. Subcomplexes were prepared in vitro by incubating the resolved E2, a 24-subunit cube-shaped molecule, with E1 (dimeric). The morphology and mass of the subcomplexes were determined by scanning transmission electron microscopy of negatively stained and of freeze-dried specimens. Images of both negative stained and freeze-dried subcomplexes were consistent with E1 binding at or near the midpoints of the edges of the E2 molecule. Mass analysis of the freeze-dried specimen showed that at least 95% of E1 remains in the dimeric state (or as two closely juxtaposed monomers) when it binds to E2.

Source: Journal of Biological Chemistry

DOI: 10.1016/s0021-9258(19)75868-2

Authors: T Wagenknecht, N Francis, D J DeRosier, J F Hainfeld, J S Wall

Institutions: Brookhaven National Laboratory, New York State Department of Health, Wadsworth Center, Brandeis University

Language: English

Topic: Biochemical Acid Research Studies

Subfield: Biochemistry

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $3,430

Funders: National Institute of General Medical Sciences, National Center for Research Resources