Succinate Dhydrogenase Mutants of Bacillus Suybtilis Lacking Covalently Bound Flavin in the Flavoprotien Subunit

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Abstract
Succinate dehydrogenase consists of 2 unequal subunits: Fp and Ip. An FAD group is covalently linked to a histidyl residue in the Fp subunit. The mechanism by which flavin is attached to protein is not known. Covalently bound flavin was studied in wild-type and succinate-dehydrogenase-negative B. subtilis. The Fp subunit of succinate dehydrogenase is the only (major) flavinylated protein in the cell. Mutants lacking covalently bound flavin and still containing the Fp polypeptide are described. The flavin is not essential for assembly and membrane binding of succinate dehydrogenase in B. subtilis.