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ferric reductase-like transmembrane domain-containing protein
This family includes a common region in the transmembrane proteins mammalian cytochrome B-245 heavy chain (gp91-phox), ferric reductase transmembrane component in yeast and respiratory burst oxidase from mouse-ear cress. This may be a family of flavocytochromes capable of moving electrons across the plasma membrane [1]. The Frp1 protein Swiss:Q04800 from S. pombe is a ferric reductase component and is required for cell surface ferric reductase activity, mutants in frp1 are deficient in ferric iron uptake [1]. Cytochrome B-245 heavy chain Swiss:P04839 is a FAD-dependent dehydrogenase it is also has electron transferase activity which reduces molecular oxygen to superoxide anion, a precursor in the production of microbicidal oxidants [2]. Mutations in the sequence of cytochrome B-245 heavy chain (gp91-phox) lead to the X-linked chronic granulomatous disease. The bacteriocidal ability of phagocytic cells is reduced and is characterised by the absence of a functional plasma membrane associated NADPH oxidase [3]. The chronic granulomatous disease gene codes for the beta chain of cytochrome B-245 and cytochrome B-245 is missing from patients with the disease [4]. [1]. 8321236. The fission yeast ferric reductase gene frp1+ is required for ferric iron uptake and encodes a protein that is homologous to the gp91-phox subunit of the human NADPH phagocyte oxidoreductase. Roman DG, Dancis A, Anderson GJ, Klausner RD;. Mol Cell Biol 1993;13:4342-4350. [2]. 1318579. Cytochrome b558: the flavin-binding component of the phagocyte NADPH oxidase. Rotrosen D, Yeung CL, Leto TL, Malech HL, Kwong CH;. Science 1992;256:1459-1462. [3]. 3600768. . TRUNCATED at 1650 bytes (from Pfam)
protein-methionine-sulfoxide reductase heme-binding subunit MsrQ
protein-methionine-sulfoxide reductase heme-binding subunit MsrQ is part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons
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