Purification and characterization of ferredoxin-NADP+ reductase encoded by Bacillus subtilis yumC

• Published in: Archives of microbiology Vol. 182; no. 1; pp. 80 - 89
• Main Authors: SEO, Daisuke, KAMINO, Kei, INOUE, Kazuhito, SAKURAI, Hidehiro
• Format: Journal Article
• Language: English
• Published: Heidelberg Springer 01.09.2004; Berlin Springer Nature B.V
• Subjects: Amino acids; Bacillus subtilis - enzymology; Bacillus subtilis - genetics; Bacteria; Biological and medical sciences; Enzymes; Ferredoxin-NADP Reductase - chemistry; Ferredoxin-NADP Reductase - genetics; Ferredoxin-NADP Reductase - isolation & purification; Ferredoxins - metabolism; Fundamental and applied biological sciences. Psychology; Gram-positive bacteria; Microbiology; Phylogeny; Purification; Ferredoxin-NADP+ reductase; Microbiology; Enzyme; Bacillus subtilis; Oxidase; yumC; NADPH-thioredoxin reductase; Bacillaceae; Thioredoxin; reductase; Bacillales; NADPH oxidase; Bacteria; Ferredoxin-NADP; Oxidoreductases; Ferredoxin

From Bacillus subtilis cell extracts, ferredoxin-NADP+ reductase (FNR) was purified to homogeneity and found to be the yumC gene product by N-terminal amino acid sequencing. YumC is a approximately 94-kDa homodimeric protein with one molecule of non-covalently bound FAD per subunit. In a diaphorase...