On the nature of the iron sulfur cluster in a deuterated algal ferredoxin.
A protonated and a completely deuterated two-iron algal ferredoxin from Synechococcus lividus have been studied by optical, electron paramagnetic resonance, electron-nuclear double resonance, proton magnetic resonance and Mossbauer spectroscopies; temperature dependent magnetic susceptibility measurements are reported as well. These studies have confirmed the electron localized model of the active center in the two-iron ferredoxins, as previously deduced from studies of spinach ferredoxin, have yielded much more precise spectroscopic parameters for this center, and have thus greatly increased the confidence in this model.
D001665:Binding Sites; D003903:Deuterium; D004578:Electron Spin Resonance Spectroscopy; D056890:Eukaryota; D005288:Ferredoxins; D007501:Iron; D009682:Magnetic Resonance Spectroscopy; D008280:Magnetics; D011485:Protein Binding; D011487:Protein Conformation; D013455:Sulfur; D013696:Temperature
D005288:Ferredoxins; D013455:Sulfur; D003903:Deuterium; D007501:Iron