<?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%">Moura, I.</style></author><author><style face="normal" font="default" size="100%">Tavares, P</style></author><author><style face="normal" font="default" size="100%">Moura, J. J.</style></author><author><style face="normal" font="default" size="100%">Ravi, N.</style></author><author><style face="normal" font="default" size="100%">Huynh, B. H.</style></author><author><style face="normal" font="default" size="100%">Liu, M. Y.</style></author><author><style face="normal" font="default" size="100%">Legall, J.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Purification and characterization of desulfoferrodoxin. A novel protein from Desulfovibrio desulfuricans (ATCC 27774) and from Desulfovibrio vulgaris (strain Hildenborough) that contains a distorted rubredoxin center and a mononuclear ferrous center</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%">Desulfovibrio/*analysis</style></keyword><keyword><style  face="normal" font="default" size="100%">Electron Spin Resonance Spectroscopy</style></keyword><keyword><style  face="normal" font="default" size="100%">Ferredoxins/chemistry/*isolation &amp; purification</style></keyword><keyword><style  face="normal" font="default" size="100%">Iron/analysis</style></keyword><keyword><style  face="normal" font="default" size="100%">Molecular Sequence Data</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%">Peptide Fragments/chemistry</style></keyword><keyword><style  face="normal" font="default" size="100%">Spectrum Analysis</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1990</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Dec 15</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=2174880 </style></url></web-urls></urls><number><style face="normal" font="default" size="100%">35</style></number><volume><style face="normal" font="default" size="100%">265</style></volume><pages><style face="normal" font="default" size="100%">21596-602</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;A new type of non-heme iron protein was purified to homogeneity from extracts of Desulfovibrio desulfuricans (ATCC 27774) and Desulfovibrio vulgaris (strain Hildenborough). This protein is a monomer of 16-kDa containing two iron atoms per molecule. The visible spectrum has maxima at 495, 368, and 279 nm and the EPR spectrum of the native form shows resonances at g = 7.7, 5.7, 4.1 and 1.8 characteristic of a high-spin ferric ion (S = 5/2) with E/D = 0.08. Mossbauer data indicates the presence of two types of iron: an FeS4 site very similar to that found in desulforedoxin from Desulfovibrio gigas and an octahedral coordinated high-spin ferrous site most probably with nitrogen/oxygen-containing ligands. Due to this rather unusual combination of active centers, this novel protein is named desulfoferrodoxin. Based on NH2-terminal amino acid sequence determined so far, the desulfoferrodoxin isolated from D. desulfuricans (ATCC 27774) appears to be a close analogue to a recently discovered gene product from D. vulgaris (Brumlik, M.J., and Voordouw, G. (1989) J. Bacteriol. 171, 49996-50004), which was suggested to be a rubredoxin oxidoreductase. However, reduced pyridine nucleotides failed to reduce the desulforedoxin-like center of this new protein.&lt;/p&gt;
</style></abstract><accession-num><style face="normal" font="default" size="100%">2174880</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, Non-P.H.S.Research Support, U.S. Gov't, P.H.S.&lt;/p&gt;
</style></notes><auth-address><style face="normal" font="default" size="100%">Centro de Tecnologia Quimica e Biologica, Oeiras, Portugal.</style></auth-address></record></records></xml>