Characterization of lipoamide dehydrogenase from Escherichia coli lacking the redox active disulfide: C44S and C49S.
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[1] Wade H. Shafer,et al. Chemistry and Biochemistry , 1997 .
[2] C. Williams,et al. Lipoamide dehydrogenase from Escherichia coli lacking the redox active disulfide: C44S and C49S. Redox properties of the FAD and interactions with pyridine nucleotides. , 1995, Biochemistry.
[3] J. Guest,et al. Properties of lipoamide dehydrogenase altered by site-directed mutagenesis at a key residue (I184Y) in the pyridine nucleotide binding domain. , 1991, Biochemistry.
[4] N. Scrutton,et al. Directed mutagenesis of the redox-active disulphide bridge in glutathione reductase from Escherichia coli , 1990, Proceedings of the Royal Society of London. Series B: Biological Sciences.
[5] P. Karplus,et al. Substrate binding and catalysis by glutathione reductase as derived from refined enzyme: substrate crystal structures at 2 A resolution. , 1994, Journal of molecular biology.
[6] J. Guest,et al. Oligonucleotide‐Directed Mutagenesis of the lpd Gene of Escherichia coli , 1989 .
[7] L. Sahlman,et al. Properties of Lipoamide Dehydrogenase and Thioredoxin Reductase from Escherichia coli Altered by Site‐Directed Mutagenesis a , 1989, Annals of the New York Academy of Sciences.
[8] L. Sahlman,et al. Lipoamide dehydrogenase from Escherichia coli. Steady-state kinetics of the physiological reaction. , 1989, The Journal of biological chemistry.
[9] G. Vriend,et al. X-ray structure of lipoamide dehydrogenase from Azotobacter vinelandii determined by a combination of molecular and isomorphous replacement techniques. , 1989, Journal of molecular biology.
[10] C. Walsh,et al. Mutagenesis of the redox-active disulfide in mercuric ion reductase: catalysis by mutant enzymes restricted to flavin redox chemistry. , 1989, Biochemistry.
[11] J. Guest,et al. Overexpression and mutagenesis of the lipoamide dehydrogenase of Escherichia coli. , 1988, The Biochemical journal.
[12] P. Karplus,et al. Refined structure of glutathione reductase at 1.54 A resolution. , 1987, Journal of molecular biology.
[13] J. Shafer,et al. Reactivity of small thiolate anions and cysteine-25 in papain toward methyl methanethiosulfonate. , 1986, Biochemistry.
[14] P. Schultz,et al. Directed mutagenesis of the redox-active disulfide in the flavoenzyme mercuric ion reductase. , 1985, Biochemistry.
[15] C. Williams,et al. Reconstitution of Escherichia coli thioredoxin reductase with 1-deazaFAD. Evidence for 1-deazaFAD C-4a adduct formation linked to the ionization of an active site base. , 1984, The Journal of biological chemistry.
[16] L. Polgár,et al. Current problems in mechanistic studies of serine and cysteine proteinases. , 1982, The Biochemical journal.
[17] C. Thorpe,et al. Lipoamide dehydrogenase from pig heart. Pyridine nucleotide induced changes in monoalkylated two-electron reduced enzyme. , 1981, Biochemistry.
[18] K. Wilkinson,et al. NADH inhibition and NAD activation of Escherichia coli lipoamide dehydrogenase catalyzing the NADH-lipoamide reaction. , 1981, The Journal of biological chemistry.
[19] K. Wilkinson,et al. Evidence for multiple electronic forms of two-electron-reduced lipoamide dehydrogenase from Escherichia coli. , 1979, The Journal of biological chemistry.
[20] C. Thorpe,et al. Spectral evidence for a flavin adduct in a monoalkylated derivative of pig heart lipoamide dehydrogenase. , 1976, The Journal of biological chemistry.
[21] R. Matthews,et al. Measurement of the oxidation-reduction potentials for two-electron and four-electron reduction of lipoamide dehydrogenase from pig heart. , 1976, The Journal of biological chemistry.
[22] C. Thorpe,et al. Differential reactivity of the two active site cysteine residues generated on reduction of pig heart lipoamide dehydrogenase. , 1976, The Journal of biological chemistry.
[23] G. L. Kenyon,et al. Simple alkanethiol groups for temporary blocking of sulfhydryl groups of enzymes. , 1975, Biochemistry.
[24] D. Lambeth,et al. The kinetics and mechanism of reduction of electron transfer proteins and other compounds of biological interest by dithionite. , 1973, The Journal of biological chemistry.
[25] U. K. Laemmli,et al. Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 , 1970, Nature.
[26] C. Williams,et al. A method for titrating oxygen-sensitive organic redox systems with reducing agents in solution. , 1969, Analytical biochemistry.
[27] G. Zanetti,et al. Characterization of the active center of thioredoxin reductase. , 1967, The Journal of biological chemistry.
[28] Williams Ch. Studies on lipoyl dehydrogenase from Escherichia coli. , 1965 .
[29] B. Anderson,et al. THE THIONICOTINAMIDE ANALOGS OF DPN AND TPN. I. PREPARATION AND ANALYSIS. , 1963, Biochemistry.
[30] V. Massey,et al. The reaction mechanism of lipoamide dehydrogenase. II. Modification by trace metals. , 1962, Biochimica et biophysica acta.
[31] V. Massey,et al. Studies on the reaction mechanism of lipoyl dehydrogenase. , 1961, Biochimica et biophysica acta.
[32] Q. Gibson,et al. Intermediates in the catalytic action of lipoyl dehydrogenase (diaphorase). , 1960, The Biochemical journal.
[33] L. Reed,et al. alpha-Keto acid dehydrogenation complexes. III. Purification and properties of dihydrolipoic dehydrogenase of Escherichia coli. , 1960, The Journal of biological chemistry.
[34] V MASSEY,et al. The identity of diaphorase and lipoyl dehydrogenase. , 1958, Biochimica et biophysica acta.
[35] H. Beinert,et al. On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A. VI. Isolation and properties of stable enzyme-substrate complexes. , 1958, The Journal of biological chemistry.
[36] V. Massey. The identity of diaphorase and lipoic dehydrogenase. , 1958, Biochimica et biophysica acta.
[37] K. Foley,et al. MOLECULAR INTERACTION OF ISOALLOXAZINE DERIVATIVES. , 1958, Proceedings of the National Academy of Sciences of the United States of America.
[38] F. B. Straub,et al. Isolation and properties of a flavoprotein from heart muscle tissue. , 1939, The Biochemical journal.