Results 151 to 160 of about 9,715 (195)

Microbial Alcohol, Aldehyde and Formate Ester Oxidoreductases

1993
Formation of alcohols by natural processes takes place in the fermentative breakdown of sugars and the oxidative dissimilation of alkanes. In view of the wide-spreadness of these processes, it is understandable that many microbial species have the capacity to degrade these compounds.
P W, van Ophem, J A, Duine
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Structure of a Hyperthermophilic Tungstopterin Enzyme, Aldehyde Ferredoxin Oxidoreductase

Science, 1995
The crystal structure of the tungsten-containing aldehyde ferredoxin oxidoreductase (AOR) from Pyrococcus furiosus , a hyperthermophilic archaeon (formerly archaebacterium) that grows optimally at 100°C, has been determined at 2.3 angstrom resolution by means of multiple isomorphous replacement and multiple crystal ...
Chan, Michael K., Mukund, Swarnalatha, Kletzin, Arnulf, Adams, Michael W. W., Rees, Douglas C.   +4 more
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[11] Aldehyde Oxidoreductases from Pyrococcus furiosus

2001
Publisher Summary An early study with Pyrococcus furiosus showed that growth of this hyperthermophilic archaeon is stimulated by the addition of tungsten to the medium. Subsequently, three distinct tungsten-containing enzymes were purified from this and related organisms.
Roopali Roy, Angeli L. Menon, Michael W.W. Adams   +2 more
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Microbial Alcohol/Aldehyde Oxidoreductases in Enantioselective Conversions

1992
Microbes have an enormous diversity of alcohol and aldehyde oxidoreductases. A brief overview is given of the types known and of some novel ones discovered recently. Except from the classical, NAD-dependent, alcohol dehydrogenase (the long chain, zinc-containing type, EC 1.1.1.1), these enzymes are unexplored with respect to enantioselectivity.
A. Geerlof, J. B. A. Tol, J. A. Jongejan, J. A. Duine   +3 more
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On a reversible molybdenum-containing aldehyde oxidoreductase from Clostridium formicoaceticum

Archives of Microbiology, 1993
Clostridium 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, Claudia Huber, Richard Feicht, Helmut Simon   +3 more
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Modelling the Electron‐Transfer Complex Between Aldehyde Oxidoreductase and Flavodoxin

European Journal of Inorganic Chemistry, 2006
AbstractThree‐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, P. Nuno Palma, Isabel Moura, José J. G. Moura   +3 more
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Comparative localization of aldehyde oxidase and xanthine oxidoreductase activity in rat tissues

The Histochemical Journal, 1998
The distribution of aldehyde oxidase activity was evaluated in unfixed cryostat sections from tissues of male Wistar rats using a tissue protectant, polyvinyl alcohol, with Tetranitro BT as a final electron acceptor. The distribution of aldehyde oxidase activity was compared with that of xanthine oxidoreductase.
Y, Moriwaki, T, Yamamoto, J, Yamakita, S, Takahashi, K, Higashino   +4 more
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Structure refinement of the aldehyde oxidoreductase from Desulfovibrio gigas (MOP) at 1.28 Å

JBIC Journal of Biological Inorganic Chemistry, 2001
The 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, J, Dias, R, Huber, J, Moura, M, Romão   +4 more
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The Tungsten-Containing Aldehyde Oxidoreductase fromClostridium thermoaceticumand its Complex with a Viologen-Accepting NADPH Oxidoreductase

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, R, Feicht, H, White, F, Lottspeich, H, Simon   +4 more
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Tungsten-containing aldehyde oxidoreductase of Eubacterium acidaminophilum.

European journal of biochemistry, 2004
Aldehyde 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, Andrea, Graentzdoerffer, Katrin, Granderath, Jan R, Andreesen, Andreas, Pich   +4 more
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