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Wistar rats of both sexes, 8 weeks old, were acquired and maintained under standard bioterium conditions (25C, 55% humidity and 12:12 h light and dark photoperiod) with water and food ad libitum

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Mutations of the residues relating to FAD-binding, ubiquinone-binding or FAD hydroxylation pockets reduced the NADH oxidation activity of FSP1 proteins (Supplementary Table 2), among which K117A, K292A/M293A/Y295A, R53A mutations of cFSP1 were almost completely inactive in vitro

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