Results 151 to 160 of about 6,446 (181)

A Biosensor for Aromatic Aldehydes Comprising the Mediator Dependent PaoABC‐Aldehyde Oxidoreductase

Electroanalysis, 2012
AbstractA novel aldehyde oxidoreductase (PaoABC) from Escherichia coli was utilized for the development of an oxygen insensitive biosensor for benzaldehyde. The enzyme was immobilized in polyvinyl alcohol and currents were measured for aldehyde oxidation with different one and two electron mediators with the highest sensitivity for benzaldehyde in the ...
Badalyan, Artavazd, Neumann-Schaal, Meina, Leimkühler, Silke (Prof. Dr.), Wollenberger, Ursula (Prof. Dr.)   +3 more
openaire   +2 more sources

[4] Aldehyde oxidoreductases and other molybdenum-containing enzymes

Methods in Enzymology, 1994
JOSÉ J G Moura
exaly   +2 more sources

Aldehyde oxidoreductase as a biocatalyst: Reductions of vanillic acid

Enzyme and Microbial Technology, 2008
Aldehyde oxidoreductase (carboxylic acid reductase) catalyzes the Mg(2+), ATP and NADPH dependent reduction of carboxylic acids to their corresponding aldehydes. The identification of the gene from Nocardia sp. NRRL 5646 and its expression in E.
Padmesh, Venkitasubramanian, Lacy, Daniels, Shuvendu, Das, Andrew S, Lamm, John P N, Rosazza   +4 more
openaire   +2 more sources

[11] Aldehyde Oxidoreductases from Pyrococcus furiosus

Methods in Enzymology, 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, Michael W W Adams
exaly   +2 more sources

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
openaire   +3 more sources

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
openaire   +2 more sources

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
openaire   +3 more sources

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
openaire   +1 more source

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
openaire   +1 more source

Aldehyde oxidoreductase activity in Desulfovibrio gigas: In vitro reconstitution of an electron-transfer chain from aldehydes to the production of molecular hydrogen

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
openaire   +2 more sources