<?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%">Archer, M.</style></author><author><style face="normal" font="default" size="100%">Carvalho, A. L.</style></author><author><style face="normal" font="default" size="100%">Teixeira, S.</style></author><author><style face="normal" font="default" size="100%">Moura, I.</style></author><author><style face="normal" font="default" size="100%">Moura, J. J.</style></author><author><style face="normal" font="default" size="100%">Rusnak, F.</style></author><author><style face="normal" font="default" size="100%">Romao, M. J.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Structural studies by X-ray diffraction on metal substituted desulforedoxin, a rubredoxin-type protein</style></title><secondary-title><style face="normal" font="default" size="100%">Protein Sci</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%">Bacterial Proteins/*chemistry</style></keyword><keyword><style  face="normal" font="default" size="100%">Crystallography, X-Ray</style></keyword><keyword><style  face="normal" font="default" size="100%">Iron-Sulfur Proteins/*chemistry</style></keyword><keyword><style  face="normal" font="default" size="100%">Metals/*chemistry</style></keyword><keyword><style  face="normal" font="default" size="100%">Models, Molecular</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Sequence Data</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Conformation</style></keyword><keyword><style  face="normal" font="default" size="100%">Recombinant Proteins/chemistry</style></keyword><keyword><style  face="normal" font="default" size="100%">Rubredoxins/chemistry</style></keyword><keyword><style  face="normal" font="default" size="100%">Sequence Homology, Amino Acid</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1999</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Jul</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=10422844 </style></url></web-urls></urls><number><style face="normal" font="default" size="100%">7</style></number><volume><style face="normal" font="default" size="100%">8</style></volume><pages><style face="normal" font="default" size="100%">1536-45</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Desulforedoxin (Dx), isolated from the sulfate reducing bacterium Desulfovibrio gigas, is a small homodimeric (2 x 36 amino acids) protein. Each subunit contains a high-spin iron atom tetrahedrally bound to four cysteinyl sulfur atoms, a metal center similar to that found in rubredoxin (Rd) type proteins. The simplicity of the active center in Dx and the possibility of replacing the iron by other metals make this protein an attractive case for the crystallographic analysis of metal-substituted derivatives. This study extends the relevance of Dx to the bioinorganic chemistry field and is important to obtain model compounds that can mimic the four sulfur coordination of metals in biology. Metal replacement experiments were carried out by reconstituting the apoprotein with In3+, Ga3+, Cd2+, Hg2+, and Ni2+ salts. The In3+ and Ga3+ derivatives are isomorphous with the iron native protein; whereas Cd2+, Hg2+, and Ni2+ substituted Dx crystallized under different experimental conditions, yielding two additional crystal morphologies; their structures were determined by the molecular replacement method. A comparison of the three-dimensional structures for all metal derivatives shows that the overall secondary and tertiary structures are maintained, while some differences in metal coordination geometry occur, namely, bond lengths and angles of the metal with the sulfur ligands. These data are discussed in terms of the entatic state theory.&lt;/p&gt;
</style></abstract><accession-num><style face="normal" font="default" size="100%">10422844</style></accession-num><notes><style face="normal" font="default" size="100%">&lt;p&gt;0961-8368 (Print)0961-8368 (Linking)Journal ArticleResearch Support, Non-U.S. Gov't&lt;/p&gt;
</style></notes><auth-address><style face="normal" font="default" size="100%">Departamento de Quimica, Centro de Quimica Fina e Biotechnologia, Faculdade de Ciencias e Tecnologia, Universidade Nova de Lisboa, Caparica, Portugal.</style></auth-address></record></records></xml>