<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Duarte, R. O.</style></author><author><style face="normal" font="default" size="100%">Archer, M.</style></author><author><style face="normal" font="default" size="100%">Dias, J. M.</style></author><author><style face="normal" font="default" size="100%">Bursakov, S.</style></author><author><style face="normal" font="default" size="100%">Huber, R.</style></author><author><style face="normal" font="default" size="100%">Moura, I.</style></author><author><style face="normal" font="default" size="100%">Romao, M. J.</style></author><author><style face="normal" font="default" size="100%">Moura, J. J.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Biochemical/spectroscopic characterization and preliminary X-ray analysis of a new aldehyde oxidoreductase isolated from Desulfovibrio desulfuricans ATCC 27774</style></title><secondary-title><style face="normal" font="default" size="100%">Biochem Biophys Res Commun</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">*Coenzymes</style></keyword><keyword><style  face="normal" font="default" size="100%">Aldehyde Oxidoreductases/*chemistry/*isolation &amp; purification/metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Crystallography, X-Ray</style></keyword><keyword><style  face="normal" font="default" size="100%">Desulfovibrio/*enzymology</style></keyword><keyword><style  face="normal" font="default" size="100%">Dimerization</style></keyword><keyword><style  face="normal" font="default" size="100%">Electron Spin Resonance Spectroscopy</style></keyword><keyword><style  face="normal" font="default" size="100%">Metalloproteins/chemistry</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Weight</style></keyword><keyword><style  face="normal" font="default" size="100%">Oxidation-Reduction</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Structure, Quaternary</style></keyword><keyword><style  face="normal" font="default" size="100%">Pteridines/chemistry</style></keyword><keyword><style  face="normal" font="default" size="100%">Spectrophotometry</style></keyword><keyword><style  face="normal" font="default" size="100%">Substrate Specificity</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2000</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Feb 24</style></date></pub-dates></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&amp;db=PubMed&amp;dopt=Citation&amp;list_uids=10679276 </style></url></web-urls></urls><number><style face="normal" font="default" size="100%">3</style></number><volume><style face="normal" font="default" size="100%">268</style></volume><pages><style face="normal" font="default" size="100%">745-9</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Aldehyde oxidoreductase (AOR) activity has been found in different sulfate reducing organisms (Moura, J. J. G., and Barata, B. A. S. (1994) in Methods in Enzymology (Peck, H. D., Jr., and LeGall, J., Eds.), Vol. 243, Chap. 4. Academic Press; Romao, M. J., Knablein, J., Huber, R., and Moura, J. J. G. (1997) Prog. Biophys. Mol. Biol. 68, 121-144). The enzyme was purified to homogeneity from extracts of Desulfovibrio desulfuricans (Dd) ATCC 27774, a sulfate reducer that can use sulfate or nitrate as terminal respiratory substrates. The protein (AORDd) is described as a homodimer (monomer, circa 100 kDa), contains a Mo-MCD pterin, 2 x [2Fe-2S] clusters, and lacks a flavin group. Visible and EPR spectroscopies indicate a close similarity with the AOR purified from Desulfovibrio gigas (Dg) (Barata, B. A. S., LeGall, J., and Moura, J. J. G. (1993) Biochemistry 32, 11559-11568). Activity and substrate specificity for different aldehydes were determined. EPR studies were performed in native and reduced states of the enzyme and after treatment with ethylene glycol and dithiothreitol. The AORDd was crystallized using ammonium sulfate as precipitant and the crystals belong to the space group P6(1)22, with unit cell dimensions a = b = 156.4 and c = 177.1 A. These crystals diffract to beyond 2.5 A resolution and a full data set was measured on a rotating anode generator. The data were used to solve the structure by Patterson Search methods, using the model of AORDg.&lt;/p&gt;
</style></abstract><accession-num><style face="normal" font="default" size="100%">10679276</style></accession-num><notes><style face="normal" font="default" size="100%">&lt;p&gt;0006-291X (Print)0006-291X (Linking)Journal Article&lt;/p&gt;
</style></notes><auth-address><style face="normal" font="default" size="100%">Departamento de Quimica (and Centro de Quimica Fina e Biotecnologia), Universidade Nova de Lisboa, Monte de Caparica, 2825-114, Portugal.</style></auth-address></record></records></xml>