Mössbauer effect and electron paramagnetic resonance studies on yeast aconitase.
Mössbauer effect and electron paramagnetic resonance (EPR) were measured for yeast aconitase [EC 4.2.1.3] purified from the cells of Candida lipolytica (ATCC 200114). Mössbauer spectra suggested that yeast aconitase nostly contained two high-spin Fe(III) ions in an antiferromagnetically coupled binuclear complex that resembled oxidized 2 Fe ferredoxins, together with a small amount of high-spin Fe(II). EPR spectra recorded no signal at 77degreesK, but showed a slightly asymmetric signal centered at g=2.0 at 4.2degreesK, presumably due to the small amount of Fe(II) Fe(III) pairs.
D000154:Aconitate Hydratase; D001665:Binding Sites; D002175:Candida / Q000201:enzymology*; D004578:Electron Spin Resonance Spectroscopy; D006836:Hydro-Lyases; D007501:Iron / Q000032:analysis; D011485:Protein Binding; D011487:Protein Conformation; D013057:Spectrum Analysis; D013455:Sulfur / Q000032:analysis; D013696:Temperature
D013455:Sulfur; D007501:Iron; D006836:Hydro-Lyases; D000154:Aconitate Hydratase