<?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%">Czaja, C.</style></author><author><style face="normal" font="default" size="100%">Litwiller, R.</style></author><author><style face="normal" font="default" size="100%">Tomlinson, A. J.</style></author><author><style face="normal" font="default" size="100%">Naylor, S.</style></author><author><style face="normal" font="default" size="100%">Tavares, P</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><author><style face="normal" font="default" size="100%">Moura, I.</style></author><author><style face="normal" font="default" size="100%">Rusnak, F.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Expression of Desulfovibrio gigas desulforedoxin in Escherichia coli. Purification and characterization of mixed metal isoforms</style></title><secondary-title><style face="normal" font="default" size="100%">J Biol Chem</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Amino Acid Sequence</style></keyword><keyword><style  face="normal" font="default" size="100%">Amino Acids/analysis</style></keyword><keyword><style  face="normal" font="default" size="100%">Bacterial Proteins/biosynthesis</style></keyword><keyword><style  face="normal" font="default" size="100%">Base Sequence</style></keyword><keyword><style  face="normal" font="default" size="100%">Binding Sites</style></keyword><keyword><style  face="normal" font="default" size="100%">Cloning, Molecular</style></keyword><keyword><style  face="normal" font="default" size="100%">Desulfovibrio/genetics/*metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA Primers</style></keyword><keyword><style  face="normal" font="default" size="100%">Electron Spin Resonance Spectroscopy/methods</style></keyword><keyword><style  face="normal" font="default" size="100%">Escherichia coli</style></keyword><keyword><style  face="normal" font="default" size="100%">Genes, Bacterial</style></keyword><keyword><style  face="normal" font="default" size="100%">Iron-Sulfur Proteins/*biosynthesis/*chemistry/isolation &amp; purification</style></keyword><keyword><style  face="normal" font="default" size="100%">Iron/analysis/*metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Mass Spectrometry</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Sequence Data</style></keyword><keyword><style  face="normal" font="default" size="100%">Polymerase Chain Reaction</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Structure, Tertiary</style></keyword><keyword><style  face="normal" font="default" size="100%">Recombinant Proteins/biosynthesis/chemistry/isolation &amp; purification</style></keyword><keyword><style  face="normal" font="default" size="100%">Spectrophotometry</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1995</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Sep 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=7657596 </style></url></web-urls></urls><number><style face="normal" font="default" size="100%">35</style></number><volume><style face="normal" font="default" size="100%">270</style></volume><pages><style face="normal" font="default" size="100%">20273-7</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 dsr gene from Desulfovibrio gigas encoding the nonheme iron protein desulforedoxin was cloned using the polymerase chain reaction, expressed in Escherichia coli, and purified to homogeneity. The physical and spectroscopic properties of the recombinant protein resemble those observed for the native protein isolated from D. gigas. These include an alpha 2 tertiary structure, the presence of bound iron, and absorbance maxima at 370 and 506 nm in the UV/visible spectrum due to ligand-to-iron charge transfer bands. Low temperature electron paramagnetic resonance studies confirm the presence of a high-spin ferric ion with g values of 7.7, 5.7, 4.1, and 1.8. Interestingly, E. coli produced two forms of desulforedoxin containing iron. One form was identified as a dimer with the metal-binding sites of both subunits occupied by iron while the second form contained equivalent amounts of iron and zinc and represents a dimer with one subunit occupied by iron and the second with zinc.&lt;/p&gt;
</style></abstract><accession-num><style face="normal" font="default" size="100%">7657596</style></accession-num><notes><style face="normal" font="default" size="100%">&lt;p&gt;0021-9258 (Print)0021-9258 (Linking)Journal ArticleResearch Support, Non-U.S. Gov'tResearch Support, U.S. Gov't, P.H.S.&lt;/p&gt;
</style></notes><auth-address><style face="normal" font="default" size="100%">Section of Hematology Research, Mayo Clinic and Foundation, Rochester, Minnesota 55905, USA.</style></auth-address></record></records></xml>