Results 151 to 160 of about 6,425 (174)
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Structure refinement of the aldehyde oxidoreductase from Desulfovibrio gigas (MOP) at 1.28 Å
JBIC Journal of Biological Inorganic Chemistry, 2001The sulfate-reducing bacterium aldehyde oxidoreductase from Desulfovibrio gigas (MOP) is a member of the xanthine oxidase family of enzymes. It has 907 residues on a single polypeptide chain, a molybdopterin cytosine dinucleotide (MCD) cofactor and two [2Fe-2S] iron-sulfur clusters.
J, Rebelo +4 more
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On a reversible molybdenum-containing aldehyde oxidoreductase from Clostridium formicoaceticum
Archives of Microbiology, 1993Clostridium formicoaceticum grown in the presence of 1 mM molybdate and about 1.5×10-5 mM tungsten (present in the 5 g yeast extract/l of the growth medium) forms two reversible aldehyde oxidoreductases in an activity ratio of about 45:55. The fraction of 45% does not bind to the octyl-Sepharose column, whereas the 55% aldehyde oxidoreductase binds to ...
Hiltrud White +3 more
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Modelling the Electron‐Transfer Complex Between Aldehyde Oxidoreductase and Flavodoxin
European Journal of Inorganic Chemistry, 2006AbstractThree‐dimensional protein structures of the xanthine oxidase family show different solutions for the problem of transferring electrons between the flavin adenine dinucleotide (FAD) group and the molybdenum cofactor. In xanthine oxidase all the cofactors lie within domains of the same protein chain, whereas in CO dehydrogenase the Fe–S centres ...
Ludwig Krippahl +3 more
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Biochemistry, 1993
The molybdenum [iron-sulfur] protein, first isolated from Desulfovibrio gigas by Moura et al. [Moura, J. J. G., Xavier, A. V., Bruschi, M., Le Gall, J., Hall, D. O., & Cammack, R. (1976) Biochem. Biophys. Res. Commun. 72, 782-789], was later shown to mediate the electronic flow from salicylaldehyde to a suitable electron acceptor, 2,6 ...
B A, Barata, J, LeGall, J J, Moura
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The molybdenum [iron-sulfur] protein, first isolated from Desulfovibrio gigas by Moura et al. [Moura, J. J. G., Xavier, A. V., Bruschi, M., Le Gall, J., Hall, D. O., & Cammack, R. (1976) Biochem. Biophys. Res. Commun. 72, 782-789], was later shown to mediate the electronic flow from salicylaldehyde to a suitable electron acceptor, 2,6 ...
B A, Barata, J, LeGall, J J, Moura
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Biological Chemistry Hoppe-Seyler, 1992
Purification of aldehyde oxidoreductase from C. thermoaceticum, the first detected enzyme able to reduce reversibly non-activated carboxylic acids to the corresponding aldehydes (White, H., Strobl, G., Feicht, R. & Simon, H. (1989) Eur. J. Biochem. 184, 89-96), results in the generation of multiple forms of the enzyme.
G, Strobl +4 more
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Purification of aldehyde oxidoreductase from C. thermoaceticum, the first detected enzyme able to reduce reversibly non-activated carboxylic acids to the corresponding aldehydes (White, H., Strobl, G., Feicht, R. & Simon, H. (1989) Eur. J. Biochem. 184, 89-96), results in the generation of multiple forms of the enzyme.
G, Strobl +4 more
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Resonance Raman study on the iron-sulfur centers of Desulfovibrio gigas aldehyde oxidoreductase
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1995Resonance Raman spectra of the molybdenum containing aldehyde oxidoreductase from Desulfovibrio gigas were recorded at liquid nitrogen temperature with various excitation wavelengths. The spectra indicate that all the iron atoms are organised in [2Fe-2S] type centers consistent with cysteine ligations. No vibrational modes involving molybdenum could be
V, Zhelyaskov +4 more
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Tungsten-containing aldehyde oxidoreductase of Eubacterium acidaminophilum.
European journal of biochemistry, 2004Aldehyde oxidoreductase of Eubacterium acidaminophilum was purified to homogeneity under strict anaerobic conditions using a four-step procedure. The purified enzyme was present as a monomer with an apparent molecular mass of 67 kDa and contained 6.0 +/- 0.1 iron, 1.1 +/- 0.2 tungsten, about 0.6 mol pterin cofactor and zinc, but no molybdenum.
David, Rauh +4 more
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Potential applications of an alcohol-aldehyde/ketone oxidoreductase from thermophilic bacteria
Enzyme and Microbial Technology, 1981Practical uses of a novel alcohol dehydrogenase from Thermoanaerobium brockii have been examined in crude and purified form. Stoichiometric reduction of NADP (50 mg) was demonstrated with agarose-immobilized enzyme and 0.3 (v/v) 2-propanol solution as reductant.
R.J. Lamed, E. Keinan, J.G. Zeikus
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Tungsten-Dependent Aldehyde Oxidoreductase
2002Roopali, Roy, Michael W W, Adams
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