<?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%">Turner, N.</style></author><author><style face="normal" font="default" size="100%">Barata, B.</style></author><author><style face="normal" font="default" size="100%">Bray, R. C.</style></author><author><style face="normal" font="default" size="100%">Deistung, J.</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%">The molybdenum iron-sulphur protein from Desulfovibrio gigas as a form of aldehyde oxidase</style></title><secondary-title><style face="normal" font="default" size="100%">Biochem J</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">*Aldehyde Oxidoreductases</style></keyword><keyword><style  face="normal" font="default" size="100%">Aldehyde Oxidase</style></keyword><keyword><style  face="normal" font="default" size="100%">Desulfovibrio/*enzymology</style></keyword><keyword><style  face="normal" font="default" size="100%">Electron Spin Resonance Spectroscopy</style></keyword><keyword><style  face="normal" font="default" size="100%">Molybdenum/analysis</style></keyword><keyword><style  face="normal" font="default" size="100%">Xanthine Oxidase</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1987</style></year><pub-dates><date><style  face="normal" font="default" size="100%">May 1</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=2821990 </style></url></web-urls></urls><number><style face="normal" font="default" size="100%">3</style></number><volume><style face="normal" font="default" size="100%">243</style></volume><pages><style face="normal" font="default" size="100%">755-61</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-sulphur protein originally isolated from Desulfovibrio gigas by Moura, Xavier, Bruschi, Le Gall, Hall &amp;amp; Cammack [(1976) Biochem. Biophys. Res. Commun. 72, 782-789] has been further investigated by e.p.r. spectroscopy of molybdenum(V). The signal obtained on extended reduction of the protein with sodium dithionite has been shown, by studies at 9 and 35 HGz in 1H2O and 2H2O and computer simulations, to have parameters corresponding to those of the Slow signal from the inactive desulpho form of various molybdenum-containing hydroxylases. Another signal obtained on brief reduction of the protein with small amounts of dithionite was shown by e.p.r. difference techniques to be a Rapid type 2 signal, like that from the active form of such enzymes. In confirmation that the protein is a molybdenum-containing hydroxylase, activity measurements revealed that it had aldehyde:2,6-dichlorophenol-indophenol oxidoreductase activity. No such activity towards xanthine or purine was observed. Salicylaldehyde was a particularly good substrate, and treatment of the protein with it also gave rise to the Rapid signal. Molybdenum cofactor liberated from the protein was active in the nit-1 Neurospora crassa nitrate reductase assay. It is concluded that the protein is a form of an aldehyde oxidase or dehydrogenase. From the intensity of the e.p.r. signals and from enzyme activity measurements, 10-30% of the protein in the sample examined appeared to be in the functional form. The evolutionary significance of the protein, which may represent a primitive form of the enzyme rather than a degradation product, is discussed briefly.&lt;/p&gt;
</style></abstract><accession-num><style face="normal" font="default" size="100%">2821990</style></accession-num><notes><style face="normal" font="default" size="100%">&lt;p&gt;0264-6021 (Print)0264-6021 (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%">School of Chemistry and Molecular Sciences, University of Sussex, Falmer, Brighton, U.K.</style></auth-address></record></records></xml>