Selected references on cytochrome b₅ and cytochrome b₅-like domains

Last modified: Wed Apr 14 12:59:39 BST 2004

• Abe, K., Kimura, S., Kizawa, R., Anan, F.K. and Sugita, Y. (1985) Amino acid sequences of cytochrome b₅ from human, porcine, and bovine erythrocytes and comparison with liver microsomal cytochrome b₅. J. Biochem. (Tokyo) 97, 1659-1668.
• Banci, L., Pierattelli, R. and Turner, D.L. (1995) Determination of haem electronic structure in cytochrome b₅ and metcyanomyoglobin. Eur. J. Biochem. 232, 522-527.
• Borgese, N., D'Arrigo, A., De Silvestris, M. and Pietrini, G. (1993a) NADH-cytochrome b₅ reductase and cytochrome b₅ isoforms as models for the study of post-translational targeting to the endoplasmic reticulum. FEBS Lett. 325, 70-75.
• Borgese, N., D'Arrigo, A., De Silvestris, M. and Pietrini, G. (1993b) NADH-cytochrome b₅ reductase and cytochrome b₅. The problem of posttranslational targeting to the endoplasmic reticulum. Subcell. Biochem. 21, 313-341.
• Daff, S., Ingledew, W.J., Reid, G.A. and Chapman, S.K. (1996) New insights into the catalytic cycle of flavocytochrome b₂. Biochemistry 35, 6345-6350.
• D'Arrigo, A., Manera, E., Longhi, R., and Borgese, N. (1993) The specific subcellular localization of two isoforms of cytochrome b₅ suggests novel targeting pathways. J. Biol. Chem. 268, 2802-2808.
• De Silvestris, M., D'Arrigo, A. and Borgese, N. (1995) The targeting information of the mitochondrial outer membrane isoform of cytochrome b₅ is contained within the carboxyl-terminal region. FEBS Lett. 370, 69-74.
• Dwivedi, U.N., Shiraishi, N. and Campbell, W.H. (1994) Identification of an "essential" cysteine of nitrate reductase via mutagenesis of its recombinant cytochrome b reductase domain. J. Biol. Chem. 269, 13785-13791.
• Giordano, S.J. and Steggles, A.W. (1993) Differential expression of the mRNAs for the soluble and membrane-bound forms of rabbit cytochrome b₅. Biochim. Biophys. Acta 1172, 95-100.
• Gondry, M. and Lederer, F. (1996) Functional properties of the histidine-aspartate ion pair of flavocytochrome b₂ (L-lactate dehydrogenase): Substitution of asp282 with asparagine. Biochemistry 35, 8587-8594.
• Guillemette, J.G., Barker, P.D., Eltis, L.D., Lo, T.P., Smith, M., Brayer, G.D. and Mauk, A.G. (1994) Analysis of the bimolecular reduction of ferricytochrome c by ferrocytochrome b₅ through mutagenesis and molecular modelling. Biochimie 76, 592-604.
• Hewson, R., Newbold, R.J. and Whitford, D. (1993) The expression of bovine microsomal cytochrome b₅ in Escherichia coli and a study of the solution structure and stability of variant proteins. Protein Engineering 6, 953-964.
• Hlavica, P. (1984) On the function of cytochrome b₅ in the cytochrome P-450-dependent oxygenase system. Arch. Biochem. Biophys. 228, 600-608.
• Hlavica, P., Kellermann, J., Golly, I. and Lehnerer, M. (1994) Chemical modification of Tyr34 and Tyr129 in rabbit liver microsomal cytochrome b₅ affects interaction with cytochrome P-450 2B4. Eur. J. Biochem. 224, 1039-1046.
• Holmans, P.L., Shet, M.S., Martin-Wixtrom, C.A., Fisher, C.W. and Estabrook, R.W. (1994) The high-level expression in Escherichia coli of the membrane-bound form of human and rat cytochrome b₅ and studies on their mechanism of function. Arch. Biochem. Biophys. 312, 554-565.
• Keller, R.M. and Wüthrich, K. (1980) Structural study of the heme crevice in cytochrome b₅ based on individual assignments of the ¹H-NMR lines of the heme group and selected amino acid residues. Biochim. Biophys. Acta 621, 204-217.
• Kouzaki, N., Kawashima, H., Chung, M.C. and Shimizu, S. (1995) Purification and characterization of two forms of cytochrome b₅ from an arachidonic acid-producing fungus, Mortierella hygrophila. Biochim. Biophys. Acta 1256, 319-326.
• Kula, M.E., Allay, E.R. and Rozek, C.E. (1995) Evolutionary divergence of the cytochrome b₅ gene of Drosophila. J. Mol. Evol. 41, 430-439.
• Ladokhin, A.S., Tretyachenko-Ladokhina, V.G., Holloway, P.W., Wang, L. and Steggles, A.W. (1992) Biophysical studies of cytochromes b₅ with amino acid substitutions in the membrane-binding domain. Biophys. J. 62, 79-81.
• Lederer, F. (1994) The cytochrome b₅-fold: an adaptable module. Biochimie 76, 674-692.
• Lee, K.B., La Mar, G.N., Mansfield, K.E., Smith, K.M., Pochapsky, T.C. and Sligar, S.G. (1993) Interpretation of hyperfine shift patterns in ferricytochromes b₅ in terms of angular position of the heme: a sensitive probe for peripheral heme protein interactions. Biochim. Biophys. Acta 1202, 189-199.
• Michaelson, L.V., Lazarus, C.M., Griffiths, G., Napier, J.A. and Stobart, A.K. (1998) Isolation of a ⁵-fatty acid desaturase gene from Mortierella alpina. J. Biol. Chem. 273, 19055-19059.
• Miles, C.S., Rouviere-Fourmy, N., Lederer, F., Mathews, F.S., Reid, G.A., Black, M.T. and Chapman, S.K. (1992) Tyr-143 facilitates interdomain electron transfer in flavocytochrome b₂. Biochem. J. 285, 187-192.
• Miles, C.S., Manson, F.D., Reid, G.A. and Chapman, S.K. (1993) Substitution of a haem-iron axial ligand in flavocytochrome b₂. Biochim. Biophys. Acta 1202, 82-86.
• Mitchell, A.G. and Martin, C.E. (1995) A novel cytochrome b₅-like domain is linked to the carboxyl terminus of the Saccharomyces cerevisiae ⁹ fatty acid desaturase. J. Biol. Chem. 270, 29766-29772.
• Moore, C.D. and Lecomte, J.T. (1990) Structural properties of apocytochrome b₅: presence of a stable native core. Biochemistry 29, 1984-1989.
• Newbold, R.J., Hewson, R. and Whitford, D. (1992) The thermal stability of the tryptic fragment of bovine microsomal cytochrome b₅ and a variant containing six additional residues. FEBS Lett. 314, 419-424.
• Pfeil, W. (1993) Thermodynamics of apocytochrome b₅ unfolding. Protein Science 2, 1497-1501.
• Roush, D.J., Gill, D.S. and Willson, R.C. (1994) Electrostatic potentials and electrostatic interaction energies of rat cytochrome b₅ and a simulated anion-exchange adsorbent surface. Biophys. J. 66, 1290-1300.
• Runnegar, B. (1984) Derivation of the globins from type b cytochromes. J. Mol. Evol. 21, 33-41.
• Sharp, R.E., White, P., Chapman, S.K. and Reid, G.A. (1994) Role of the interdomain hinge of flavocytochrome b₂ in intra- and inter-protein electron transfer. Biochemistry 33, 5115-5120.
• Sharp, R.E., Chapman, S.K. and Reid, G.A. (1996a) Deletions in the interdomain hinge region of flavocytochrome b₂: Effects on intraprotein electron transfer. Biochemistry 35, 891-899.
• Sharp, R.E., Chapman, S.K. and Reid, G.A. (1996b) Modulation of flavocytochrome b₂ intraprotein electron transfer via an interdomain hinge region. Biochem. J. 316, 507-513.
• Silvestrini, M.C., Sarti, P. and Tegoni, M. (1995) Reaction of the Hansenula anomala flavocytochrome b₂ and cytochrome b₂ core with inorganic outer sphere redox compounds. Biochimie 77, 531-538.
• Sinclair, R., Reid, G.A. and Chapman, S.K. (1998) Re-design of Saccharomyces cerevisiae flavocytochrome b₂: Introduction of L-mandelate dehydrogenase activity. Biochem. J. 333, 117-120.
• Sperling, P., Schmidt, H. and Heinz, E. (1995) A cytochrome-b₅-containing fusion protein similar to plant acyl lipid desaturases. Eur. J. Biochem. 232, 798-805.
• Sperling, P., Zähringer, U. and Heinz, E. (1998) A sphingolipid desaturase from higher plants. Identification of a new cytochrome b₅ fusion protein. J. Biol. Chem. 273, 28590-28596.
• Storch, E.M. and Daggett, V. (1995) Molecular dynamics simulation of cytochrome b₅: Implications for protein-protein recognition. Biochemistry 34, 9682-9693.
• Storch, E.M. and Daggett, V. (1996) Structural consequences of heme removal: Molecular dynamics simulations of rat and bovine apocytochrome b₅. Biochemistry 35, 11596-11604.
• Sun, Y.-L., Xie, Y., Wang, Y.-H., Xiao, G.-T. and Huang, Z.-H. (1996) The influence of Glu 44 and Glu 56 of cytochrome b₅ on the protein structure and interaction with cytochrome c. Protein Engineering 9, 555-558.
• Takematsu, H., Kozutsumi, Y., Suzuki, A. and Kawasaki, T. (1992) Molecular cloning of rabbit cytochrome b₅ genes: evidence for the occurrence of two separate genes encoding the soluble and microsomal forms. Biochem. Biophys. Res. Commun. 185, 845-851.
• Truan, G., Epinat, J.C., Rougeulle, C., Cullin, C. and Pompon, D. (1994) Cloning and characterization of a yeast cytochrome b₅-encoding gene which suppresses ketoconazole hypersensitivity in a NADPH-P-450 reductase-deficient strain. Gene 142, 123-127.
• Utecht, R.E. and Kurtz, D.M., Jr. (1988) Cytochrome b₅ and NADH-cytochrome-b₅ reductase from sipunculan erythrocytes. A methemerythrin reduction system from Phascolopsis gouldii. Biochim. Biophys. Acta 953, 164-178.
• Vergères, G. and Waskell, L. (1992) Expression of cytochrome b₅ in yeast and characterization of mutants of the membrane-anchoring domain. J. Biol. Chem. 267, 12583-12591.
• Vergères, G. and Waskell, L. (1995) Cytochrome b₅, its functions, structure and membrane topology. Biochimie 77, 604-620.
• Vergères, G., Chen, D.Y., Wu, F.F. and Waskell, L. (1993) The function of tyrosine 74 of cytochrome b₅. Arch. Biochem. Biophys. 305, 231-241.
• Vergères, G., Ramsden, J. and Waskell, L. (1995) The carboxyl terminus of the membrane-binding domain of cytochrome b₅ spans the bilayer of the endoplasmic reticulum. J. Biol. Chem. 270, 3414-3422.
• White, P., Manson, F.D., Brunt, C.E., Chapman, S.K. and Reid, G.A. (1993) The importance of the interdomain hinge in intramolecular electron transfer in flavocytochrome b₂. Biochem. J. 291, 89-94.
• Wu, F.F., Vergères, G. and Waskell, L. (1994) Kinetics of the reduction of cytochrome b₅ with mutations in its membrane-binding domain. Arch. Biochem. Biophys. 308, 380-306.
• Yamazaki, H., Nakano, M., Gillam, E.M.J., Bell, L.C., Guengerich, F.P. and Shimada, T. (1996) Requirements for cytochrome b₅ in the oxidation of 7-ethoxycoumarin, chlorzoxazone, aniline, and N-nitrosodimethylamine by recombinant P450 3E1 and by human liver microsomes. Biochem. Pharmacol. 52, 301-309.
• Yang, M.-X. and Cederbaum, A.I. (1995) Role of cytochrome b₅ in NADH-dependent microsomal reduction of ferric complexes, lipid peroxidation, and hydrogen peroxide generation. Arch. Biochem. Biophys. 324, 282-292.
• Yang, M.-X. and Cederbaum, A.I. (1996) Interaction of ferric complexes with NADH-cytochrome b5 reductase and cytochrome b5: Lipid peroxidation, H₂O₂ generation, and ferric reduction. Arch. Biochem. Biophys. 331, 69-78.
• Yu, Y., Yamasaki, H., Kita, K. and Takamiya, S. (1996) Purification and molecular characterization of a novel b₅-type cytochrome of the parasitic nematode, Ascaris suum. Arch. Biochem. Biophys. 328, 165-172.

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