Recombinant Human SDHB Protein Fragment (34-280) – a high-purity, functionally relevant fragment of the succinate dehydrogenase iron-sulfur subunit, encompassing key 2Fe-2S and 4Fe-4S ferredoxin domains. Ideal for investigating electron transfer mechanisms in mitochondrial complex II and related enzymatic activities.

The full-length Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, encoded by the SDHB gene, is a critical component of mitochondrial respiratory chain complex II. It facilitates electron transfer from succinate to ubiquinone (coenzyme Q) and also participates in oxidizing malate to enol-oxaloacetate, which regulates succinate dehydrogenase activity. Located in the mitochondrial inner membrane as a peripheral protein on the matrix side, this iron-sulfur protein is essential for cellular respiration and energy production. The provided fragment spans residues 34-280, covering the functional 2Fe-2S and 4Fe-4S ferredoxin domains, enabling focused studies on their specific roles in electron transport and enzyme function.