<?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%">Yu, L.</style></author><author><style face="normal" font="default" size="100%">Kennedy, M.</style></author><author><style face="normal" font="default" size="100%">Czaja, C.</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. G.</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%">Conversion of desulforedoxin into a rubredoxin center</style></title><secondary-title><style face="normal" font="default" size="100%">Biochemical And Biophysical Research Communications</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">1997</style></year></dates><number><style face="normal" font="default" size="100%">{3}</style></number><volume><style face="normal" font="default" size="100%">{231}</style></volume><pages><style face="normal" font="default" size="100%">{679-682}</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Rubredoxin and desulforedoxin both contain an Fe(S-Cys)(4) center, However the spectroscopic properties of the center in desulforedoxin differ from rubredoxin, These differences arise from a distortion of the metal site hypothesized to result from adjacent cysteine residues in the primary sequence of desulforedoxin. Two desulforedoxin mutants were generated in which either a G or P-V were inserted between adjacent cysteines. Both mutants exhibited optical spectra with maxima at 278, 345, 380, 480, and 560 nm while the low temperature X-band EPR spectra indicated high-spin Fe3+ ions with large rhombic distortions (E/D = 0.21-0.23). These spectroscopic properties are distinct from wild type desulforedoxin and virtually identical to rubredoxin. (C) 1997 Academic Press.&lt;/p&gt;
</style></abstract><notes><style face="normal" font="default" size="100%">n/a</style></notes><custom3><style face="normal" font="default" size="100%">papers2://publication/uuid/7303FCBE-0259-4CB4-897B-10527D99CC62</style></custom3><label><style face="normal" font="default" size="100%">r08498</style></label></record></records></xml>