<?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%">Barata, B. A.</style></author><author><style face="normal" font="default" size="100%">Legall, 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%">Aldehyde oxidoreductase activity in Desulfovibrio gigas: in vitro reconstitution of an electron-transfer chain from aldehydes to the production of molecular hydrogen</style></title><secondary-title><style face="normal" font="default" size="100%">Biochemistry</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Aldehyde Oxidoreductases/isolation &amp; purification/*metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Desulfovibrio/*enzymology</style></keyword><keyword><style  face="normal" font="default" size="100%">Electron Transport</style></keyword><keyword><style  face="normal" font="default" size="100%">Enzyme Stability</style></keyword><keyword><style  face="normal" font="default" size="100%">Hydrogen/*metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Kinetics</style></keyword><keyword><style  face="normal" font="default" size="100%">Substrate Specificity</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1993</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Nov 2</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=8218223 </style></url></web-urls></urls><number><style face="normal" font="default" size="100%">43</style></number><volume><style face="normal" font="default" size="100%">32</style></volume><pages><style face="normal" font="default" size="100%">11559-68</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;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., &amp;amp; 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-dichlorophenolindophenol (DCPIP) [Turner, N., Barata, B., Bray, R. C., Deistung, J., LeGall, J., &amp;amp; Moura, J. J. G. (1987) Biochem. J. 243, 755-761]. The DCPIP-dependent aldehyde oxidoreductase activity was studied in detail using a wide range of aldehydes and analogues. Steady-state kinetic analysis (KM and Vmax) was performed for acetaldehyde, propionaldehyde, benzaldehyde, and salicylaldehyde in excess DCPIP concentration, and a simple Michaelis-Menten model was shown to be applicable as a first kinetic approach. Xanthine, purine, allopurinol, and N1-methylnicotinamide (NMN) could not be utilized as enzyme substrates. DCPIP and ferricyanide were shown to be capable of cycling the electronic flow, whereas other cation and anion dyes [O2 and NAD(P)+] were not active in this process. The enzyme showed an optimal pH activity profile around 7.8. This molybdenum hydroxylase was shown to be part of an electron-transfer chain comprising four different soluble proteins from D. gigas, with a total of 11 discrete redox centers, which is capable of linking the oxidation of aldehydes to the reduction of protons.&lt;/p&gt;
</style></abstract><accession-num><style face="normal" font="default" size="100%">8218223</style></accession-num><notes><style face="normal" font="default" size="100%">&lt;p&gt;0006-2960 (Print)0006-2960 (Linking)Journal ArticleResearch Support, Non-U.S. Gov'tResearch Support, U.S. Gov't, Non-P.H.S.&lt;/p&gt;
</style></notes><auth-address><style face="normal" font="default" size="100%">Departamento de Quimica, Faculdade de Ciencias da Universidade de Lisboa, Oeiras, Portugal.</style></auth-address></record></records></xml>