Selected references on flavodoxins

Last modified: Wed Apr 14 12:35:23 BST 2004

• Cheddar, G., Meyer, T.E., Cusanovich, M.A., Stout, C.D. and Tollin, G. (1986) Electron-transfer reactions between flavodoxin semiquinone and c-type cytochromes: comparisons between various flavodoxins. Biochemistry 25, 6502-6507.
• Fitzgerald, M.P., Rogers, L.J., Rao, K.K. and Hall, D.O. (1980) Efficiency of ferredoxins and flavodoxins as mediators in systems for hydrogen evolution. Biochem. J. 192, 665-672.
• Grandori, R. and Carey, J. (1994) Six new candidate members of the /ß twisted open-sheet family detected by sequence similarity to flavodoxin. Protein Science 3, 2185-2193.
• Jenkins, C.M. and Waterman, M.R. (1999) Flavodoxin as a model for the P450-interacting domain of NADPH cytochrome P450 reductase. Drug Metab. Rev. 31, 195-203.
• Kobayashi, K. and Fox, J.L. (1978) The evolution of protein sequences by repetitious gene duplication: clostridial flavodoxin. J. Mol. Evol. 11, 233-243.
• Medina, M., Gómez-Moreno, C. and Tollin, G. (1992) Effects of chemical modification of Anabaena flavodoxin and ferredoxin-NADP⁺ reductase on the kinetics of interprotein electron transfer reactions. Eur. J. Biochem. 210, 577-583.
• Medina, M., Peleato, M.L., Mendez, E. and Gómez-Moreno, C. (1992) Identification of specific carboxyl groups on Anabaena PCC 7119 flavodoxin which are involved in the interaction with ferredoxin-NADP⁺ reductase. Eur. J. Biochem. 203, 373-379.
• Muñoz, V., Serrano, L., Jiménez, M.A. and Rico, M. (1995) Structural analysis of peptides encompassing all -helices of three /ß parallel proteins: Che-Y, flavodoxin and P21-ras: implications for -helix stability and the folding of /ß parallel proteins. J. Mol. Biol. 247, 648-669.
• Palma, P.N., Moura, I., LeGall, J., van Beeumen, J., Wampler, J.E. and Moura, J.J. (1994) Evidence for a ternary complex formed between flavodoxin and cytochrome c₃: ¹H-NMR and molecular modeling studies. Biochemistry 33, 6394-6407.
• Simondsen, R.P. and Tollin, G. (1980) Structure-function relations in flavodoxins. Mol. Cell Biochem. 33, 13-24.
• Vervoort, J., Heering, D., Peelen, S. and van Berkel, W. (1994) Flavodoxins. Methods Enzymol. 243, 188-203.
• Wakabayashi, S., Kimura, T., Fukuyama, K., Matsubara, H. and Rogers, L.J. (1989) The amino acid sequence of a flavodoxin from the eukaryotic red alga Chondrus crispus. Biochem. J. 263, 981-984.
• Zhou, Z. and Swenson, R.P. (1995) Electrostatic effects of surface acidic amino acid residues on the oxidation-reduction potentials of the flavodoxin from Desulfovibrio vulgaris (Hildenborough). Biochemistry 34, 3183-3192.

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