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Dithiol-iron-sulfur and selenium complexes: A comparison with iron sulfur proteins

✍ Scribed by Yukio Sugiura; Kazuhiko Ishizu; Tokuji Kimura; Hisashi Tanaka


Publisher
Elsevier Science
Year
1975
Weight
662 KB
Volume
4
Category
Article
ISSN
0006-3061

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✦ Synopsis


1, PButanedithiol and dithiothreitol-iron complexes exhibited simiiar optical absorption spectra to those of rubredoxins. The spectra of butanedithiol-iron-sulfur compIex showed sImIIarity to those of two iron and two labile sulfur w_hile dithiothrcitol-Iron-sulfur compbx resembIed those of eight iron and eight labile suIfur ferredoxins. The seIenium derivative of dithiothreitol dispIayed a red shift (25 nm) of its visible absorption band, as compared with the tadfur complex, whereas butanedithiol exhibited a bhre shift (10 nm). DithiothreitoI-iron complex showed a strong electron paramagnetic resonance absorption at g = 4.4. Upon addition of sulfur or sehnium, g-vaIues changed from g = 4.4 to g = 2. The g-values of dithiothreitoI-"Fe-' =S and dithio-threitoI-56Fe-80Se complexes were obtained as g, = 2,00, g, = 1.96,. and g, = 2.01, g, = 2.05, respectiveIy. Upon substitution with "'Fe or "Se, the signal line shape was sig,GfkantIy broadened. Butanedithiol-iron complex showed an absorption at g = 4.30. The corresponding sulfur and selenium derivatives had a split absorption in this region. Among these complexes, dithiothreitol-iron-seknium complex displayed spectroscopic properties most similar to those of naturally occurring ferredoxins.


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