279
Views
1
CrossRef citations to date
0
Altmetric
Original Articles

Structure and Properties of the Recombinant NADH–Cytochrome b5 Reductase of Physarum polycephalum

, , , &
Pages 783-790 | Received 06 Nov 2006, Accepted 07 Dec 2006, Published online: 22 May 2014

  • 1) Oshino, N., Imai, Y., and Sato, R., A function of cytochrome b 5 in fatty acid desaturation by rat liver microsomes. J. Biochem., 69, 155–167 (1971).
  • 2) Keyes, S. R., Alfano, J. A., Jansson, I., and Cinti, D. L., Rat liver microsomal elongation of fatty acids: possible involvement of cytochrome b 5. J. Biol. Chem., 254, 7778–7784 (1979).
  • 3) Fukushima, H., Grinstead, G. F., and Gaylor, J. L., Total enzymatic synthesis of cholesterol from lanosterol: cytochrome b 5-dependence of 4-methyl sterol oxidase. J. Biol. Chem., 256, 4822–4826 (1981).
  • 4) Onoda, M., and Hall, P. F., Cytochrome b 5 stimulates purified testicular microsomal cytochrome P450 (C21 side-chain cleavage). Biochem. Biophys. Res. Commun., 108, 454–460 (1982).
  • 5) Katagiri, M., Kagawa, N., and Waterman, M. R., The role of cytochrome b 5 in the biosynthesis of androgens by human P450c17. Arch. Biochem. Biophys., 317, 343–347 (1995).
  • 6) Yubisui, T., Miyata, T., Iwanaga, S., Tamura, M., and Takeshita, M., Complete amino acid sequence of NADH–cytochrome b 5 reductase purified from human erythrocytes. J. Biochem., 99, 407–422 (1986).
  • 7) Yubisui, T., Naitoh, Y., Zenno, S., Tamura, M., Takeshita, M., and Sakaki, Y., Molecular cloning of cDNAs of human liver and placenta NADH–cytochrome b 5 reductase. Proc. Natl. Acad. Sci. USA, 84, 3609–3613 (1987).
  • 8) Tomatsu, S., Kobayashi, Y., Yubisui, T., Orii, T., and Sakaki, Y., The organization and the complete nucleotide sequence of the human NADH–cytochrome b 5 reductase gene. Gene, 80, 353–361 (1989).
  • 9) Yubisui, T., Shirabe, K., Takeshita, M., Kobayashi, Y., Fukumaki, Y., Sakaki, Y., and Takano, T., Structural role of Serine 127 in the NADH-binding site of human NADH–cytochrome b 5 reductase. J. Biol. Chem., 266, 66–70 (1991).
  • 10) Shirabe, K., Yubisui, T., Borgese, N., Tang, C. Y., Hultquist, D. E., and Takeshita, M., Enzymatic instability of NADH–cytochrome b 5 reductase as a cause of hereditary methemoglobinemia type I (red cell type). J. Biol. Chem., 267, 20416–20421 (1992).
  • 11) Shirabe, K., Fujimoto, Y., Yubisui, T., and Takeshita, M., An in-frame deletion of codon 298 of the NADH–cytochrome b 5 reductase gene results in hereditary methemoglobinemia type II (generalized type): a functional implication for the role of the COOH-terminal region of the enzyme. J. Biol. Chem., 269, 5952–5957 (1994).
  • 12) Strittmatter, P., The reaction sequence in electron transfer in the reduced nicotineamide adenine dinucleotide–cytochrome b 5 reductase system. J. Biol. Chem., 240, 4481–4487 (1965).
  • 13) Ozols, J., Carr, S. A., and Strittmatter, P., Identification of the NH2-terminal blocking group of NADH–cytochrome b 5 reductase as myristic acid and the complete amino acid sequence of the membrane-binding domain. J. Biol. Chem., 259, 13349–13354 (1984).
  • 14) Strittmatter, P., Hackett, C., Korza, G., and Ozols, J., Characterization of the covalent cross-links of the active sites of amidinated cytochrome b 5 and NADH–cytochrome b 5 reductase. J. Biol. Chem., 265, 21709–21713 (1990).
  • 15) Minami, Y., Kohama, T., Sekimoto, Y., Akasaka, K., and Matsubara, H., Isolation and characterization of glutathione reductase from Physarum polycephalum and stage-specific expression of the enzyme in life-cycle stages with different oxidation-reduction levels. J. Eukaryot. Microbiol., 50, 317–323 (2003).
  • 16) Maekawa, A., Hayase, M., Yubisui, T., and Minami, Y., A cDNA cloned from Physarum polycephalum encodes new type of family 3 β-glucosidase that is a fusion protein containing a calx-β motif. Int. J. Biochem. Cell Biol., 38, 2164–2172 (2006).
  • 17) Nishida, H., Inaka, K., Yamanaka, M., Kaida, S., Kobayashi, K., and Miki, K., Crystal structure of NADH–cytochrome b 5 reductase from pig liver at 2.4 Å resolution. Biochemistry, 34, 2763–2767 (1995).
  • 18) Bewley, M. C., Marohnic, C. C., and Barber, M. J., The structure and biochemistry of NADH–cytochrome b 5 reductase are now consistent. Biochemistry, 40, 13574–13582 (2001).
  • 19) Bando, S., Takano, T., Yubisui, T., Shirabe, K., Takeshita, M., and Nakagawa, A., Structure of human erythrocyte NADH–cytochrome b 5 reductase. Acta Cryst., D60, 1929–1934 (2004).
  • 20) Shirabe, K., Yubisui, T., and Takeshita, M., Expression of human erythrocyte NADH–cytochrome b 5 reductase as an α-thrombin-cleavable fused protein in Escherichia coli. Biochim. Biophys. Acta, 1008, 189–192 (1989).
  • 21) Yubisui, T., and Takeshita, M., Characterization of the purified NADH–cytochrome b 5 reductase of human erythrocytes as a FAD-containing enzyme. J. Biol. Chem., 255, 2454–2456 (1980).
  • 22) Falk, J. E., Pyridine hemochromes. In “Porphyrines and Metalloporphyrines,” Elsevier Publishing, Amsterdam, p. 240 (1964).
  • 23) Yubisui, T., Takahashi, F., Takabayashi, T., Fujiwara, S., and Kawamura, K., Characterization of cytochrome b 5 in the ascidian Polyandrocarpa misakiensis and budding-specific expression. J. Biochem., 129, 709–716 (2001).
  • 24) Karplus, P. A., Daniels, M. J., and Herriott, J. R., Atomic structure of ferredoxin–NADP+ reductase: prototype for a structurally novel flavoprotein family. Science, 251, 60–66 (1991).
  • 25) Shirabe, K., Nagai, T., Yubisui, T., and Takeshita, M., Electrostatic interaction between NADH–cytochrome b 5 reductase and cytochrome b 5 studied by site-directed mutagenesis. Biochim. Biophys. Acta, 1384, 16–22 (1998).
  • 26) Shirabe, K., Yubisui, T., Nishino, T., and Takeshita, M., Role of cysteine residues in human NADH–cytochrome b 5 reductase studied by site-directed mutagenesis. J. Biol. Chem., 266, 7531–7536 (1991).
  • 27) Yubisui, T., Murakami, K., Takeshita, M., and Takano, T., Purification by hydrophobic chromatography of soluble cytochrome b 5 of human erythrocytes. Biochim. Biophys. Acta, 936, 447–451 (1988).
  • 28) Ohnishi, T., Imai, Y., and Yamasaki, I., The oxidation-reduction characteristics of cytochrome b 5 in hen liver microsomes. Arch. Biochem. Biophys., 167, 488–495 (1975).

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.