title: Ferredoxin-NADP reductase from the thermophilic hydrogen-oxidizing bacterium, Hydrogenobacter thermophilus TK-6.
abstract: The thermophilic, obligately chemolithoautotrophic hydrogen-oxidizing bacterium, Hydrogenobacter thermophilus TK-6, assimilates carbon dioxide via the reductive tricarboxylic acid cycle. Small iron-sulfur proteins, ferredoxins, play a central role as low-potential electron donors for this cycle. The fpr gene of this bacterium, encoding a putative ferredoxin-NADP(+) reductase (FNR, EC 1.18.1.2), was expressed in Escherichia coli, and the recombinant protein was purified to homogeneity. Unexpectedly, the monomeric Fpr protein contained one molecule of FMN as a prosthetic group, although FNRs from other organisms are known to contain FAD. The FMN-containing Fpr was shown to be a bona fide FNR that catalyzes a reversible redox reaction between NADP(+)/NADPH and ferredoxins.
authors: Department of Biotechnology, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo, Japan.
authors: Takeshi
authors: T
authors: Ikeda
authors: Miyuki
authors: M
authors: Nakamura
authors: Hiroyuki
authors: H
authors: Arai
authors: Masaharu
authors: M
authors: Ishii
authors: Yasuo
authors: Y
authors: Igarashi
mesh_terms: D000595:Amino Acid Sequence; D001419:Bacteria / Q000737:chemistry / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D005287:Ferredoxin-NADP Reductase / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D005486:Flavin Mononucleotide / Q000378:metabolism; D006358:Hot Temperature; D006859:Hydrogen / Q000378:metabolism*; D008969:Molecular Sequence Data; D016415:Sequence Alignment
chemical_list: D001426:Bacterial Proteins; D005486:Flavin Mononucleotide; D006859:Hydrogen; D005287:Ferredoxin-NADP Reductase