Proteomics

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Characterizing the molecular architecture of mitochondrial energy metabolism


ABSTRACT: The electron transfer chain is organized into inner mitochondrial membrane supercomplexes that promote substrate channeling and catalytic efficiency. This study shows that fatty acid oxidation enzymes physically interact with electron transfer chain supercomplexes at two points. The fatty acid oxidation trifunctional protein interacts with the NADH-binding domain of complex I of the electron transfer chain, while electron transfer flavoprotein dehydrogenase interacts with electron transfer chain complex III. These findings provide first view of an integrated molecular architecture for the major energy generating pathways in mitochondria.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Heart

SUBMITTER: Johan Palmfeldt  

LAB HEAD: Johan Palmfeldt

PROVIDER: PXD010838 | Pride | 2019-07-31

REPOSITORIES: Pride

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Publications

Mitochondrial fatty acid oxidation and the electron transport chain comprise a multifunctional mitochondrial protein complex.

Wang Yudong Y   Palmfeldt Johan J   Gregersen Niels N   Makhov Alexander M AM   Conway James F JF   Wang Meicheng M   McCalley Stephen P SP   Basu Shrabani S   Alharbi Hana H   St Croix Claudette C   Calderon Michael J MJ   Watkins Simon S   Vockley Jerry J  

The Journal of biological chemistry 20190624 33


Three mitochondrial metabolic pathways are required for efficient energy production in eukaryotic cells: the electron transfer chain (ETC), fatty acid β-oxidation (FAO), and the tricarboxylic acid cycle. The ETC is organized into inner mitochondrial membrane supercomplexes that promote substrate channeling and catalytic efficiency. Although previous studies have suggested functional interaction between FAO and the ETC, their physical interaction has never been demonstrated. In this study, using  ...[more]

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