- 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).
Full access
Structure and Properties of the Recombinant NADH–Cytochrome b5 Reductase of Physarum polycephalum
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.
Related research
People also read lists articles that other readers of this article have read.
Recommended articles lists articles that we recommend and is powered by our AI driven recommendation engine.
Cited by lists all citing articles based on Crossref citations.
Articles with the Crossref icon will open in a new tab.