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A key feature of the transition to MASH involves oxidative stress resulting from defects in mitochondrial oxidative phosphorylation (OXPHOS). Here, we show that pathological alterations in the lipid composition of the inner mitochondrial membrane (IMM) directly instigate electron transfer inefficiency to promote oxidative stress. Specifically, mitochondrial cardiolipin (CL) was downregulated with MASLD\/MASH in humans and in mice. Hepatocyte-specific CL synthase knockout (CLS-LKO) led to spontaneous and robust MASH with extensive steatotic and fibrotic phenotype. Loss of CL paradoxically increased mitochondrial respiratory capacity but also promoted electron leak primarily at sites III\n                    <jats:sub>QO<\/jats:sub>\n                    and II\n                    <jats:sub>F<\/jats:sub>\n                    of the electron transport chain (ETC), reduced the formation of I + III\n                    <jats:sub>2<\/jats:sub>\n                    + IV respiratory supercomplex, and disrupted the propensity of coenzyme Q to become reduced. 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