Selected references on iron-sulphur proteins

Last modified: Wed Apr 14 12:34:52 BST 2004

• Beckert, V., Schrauber, H., Bernhardt, R., Van Dijk, A.A., Kakoschke, C. and Wray, V. (1995) Mutational effects on the spectroscopic properties and biological activities of oxidized bovine adrenodoxin, and their structural implications. Eur. J. Biochem. 231, 226-235.
• Burova, T.V., Beckert, V., Uhlmann, H., Ristau, O., Bernhardt, R. and Pfeil, W. (1996) Conformational stability of adrenodoxin mutant proteins. Protein Science 5, 1890-1897.
• Chang, C.Y., Wu, D.A., Mohandas, T.K. and Chung, B.C. (1990) Structure, sequence, chromosomal location, and evolution of the human ferredoxin gene family. DNA Cell Biol. 9, 205-212.
• Fu, W., Drozdzewski, P.M., Davies, M.D., Sligar, S.G. and Johnson, M.K. (1992) Resonance Raman and magnetic circular dichroism studies of reduced [2Fe-2S] proteins. J. Biol. Chem. 267, 15502-15510.
• Iametti, S., Uhlmann, H., Ragg, E., Sala, N., Grinberg, A., Beckert, V., Bernhardt, R. and Bonomi, F. (1998) Cluster-iron substitution is related to structural and functional features of adrenodoxin mutants and to their redox states. Eur. J. Biochem. 251, 673-681.
• Iwahashi, J., Furuya, S., Mihara, K. and Omura, T. (1992) Characterization of adrenodoxin precursor expressed in Escherichia coli. J. Biochem. (Tokyo) 111, 451-455.
• Kagimoto, M., Kagimoto, K., Simpson, E.R. and Waterman, M.R. (1988) Transcription of the bovine adrenodoxin gene produces two species of mRNA of which only one is translated into adrenodoxin. J. Biol. Chem. 263, 8925-8928.
• Lobanov, N.A., Vlasova, T.M. and Adamovich, T.B. (1990) Comparative study of bovine adrenodoxin and renorenodoxin. Biokhimiia (Moscow) 55, 1059-1064.
• Moura, J.J.G., Macedo, A.L. and Palma, P.N. (1994) Ferredoxins. Methods Enzymol. 243, 165-188.
• Naud, I., Vincon, M., Garin, J., Gaillard, J., Forest, E. and Jouanneau, Y. (1994) Purification of a sixth ferredoxin from Rhodobacter capsulatus. Primary structure and biochemical properties. Eur. J. Biochem. 222, 933-939.
• O'Keefe, D.P., Gibson, K.J., Emptage, M.H., Lenstra, R., Romesser, J.A., Litle, P.J. and Omer, C.A. (1991) Ferredoxins from two sulfonylurea herbicide monooxygenase systems in Streptomyces griseolus. Biochemistry 30, 447-455.
• Sagara, Y., Hara, T., Ariyasu, Y., Ando, F., Tokunaga, N. and Horiuchi, T. (1992) Direct expression in Escherichia coli and characterization of bovine adrenodoxins with modified amino-terminal regions. FEBS Lett. 300, 208-212.
• Seaton, B.L. and Vickery, L.E. (1992) Expression of human ferredoxin in Saccharomyces cerevisiae: mitochondrial import of the protein and assembly of the [2Fe-2S] center. Arch. Biochem. Biophys. 294, 603-608.
• Shergill, J.K., Cammack, R., Chen, J.H., Fisher, M.J., Madden, S. and Rees, H.H. (1995) EPR spectroscopic characterization of the iron-sulphur proteins and cytochrome P-450 in mitochondria from the insect Spodoptera littoralis (cotton leafworm). Biochem. J. 307, 719-28.
• Stayton, P.S. and Sligar, S.G. (1991) Structural microheterogeneity of a tryptophan residue required for efficient biological electron transfer between putidaredoxin and cytochrome P-450cam. Biochemistry 30, 1845-1851.
• Ta, D.T. and Vickery, L.E. (1992) Cloning, sequencing, and overexpression of a [2Fe-2S] ferredoxin gene from Escherichia coli. J. Biol. Chem. 267, 11120-11125.
• Uhlmann, H. and Bernhardt, R. (1995a) Structure-function studies on mutants of adrenal ferredoxin. Endocr. Res. 21, 307-312.
• Uhlmann, H. and Bernhardt, R. (1995b) The role of threonine 54 in adrenodoxin for the properties of its iron-sulfur cluster and its electron transfer function. J. Biol. Chem. 270, 29954-29966.
• Uhlmann, H., Beckert, V., Schwarz, D. and Bernhardt, R. (1992) Expression of bovine adrenodoxin in E. coli and site-directed mutagenesis of [2Fe-2S] cluster ligands. Biochem. Biophys. Res. Commun. 188, 1131-1138.
• Uhlmann, H., Iametti, S., Vecchio, G., Bonomi, F. and Bernhardt, R. (1997) Pro108 is important for folding and stabilization of adrenal ferredoxin, but does not influence the functional properties of the protein. Eur. J. Biochem. 248, 897-902.
• Xia, B., Cheng, H., Skjeldal, L., Coghlan, V.M., Vickery, L.E. and Markley, J.L. (1995) Multinuclear magnetic resonance and mutagenesis studies of the histidine residues of human mitochondrial ferredoxin. Biochemistry 34, 180-187.
• Xia, B., Cheng, H., Bandarian, V., Reed, G.H. and Markley, J.L. (1996) Human ferredoxin: Overproduction in Escherichia coli, reconstitution in vitro, and spectroscopic studies of iron-sulfur cluster ligand cysteine-to-serine mutants. Biochemistry 35, 9488-9495.

Back to the Directory of P450-containing Systems home page:

Trieste site

Gödöllõ site