Mössbauer effect and electron paramagnetic resonance studies on yeast aconitase.
J Biochem, 1975/9;78(3):555-60.
Suzuki Y, Maeda Y, Sakai H, Fujimoto S, Morita Y
PMID: 178642
Impact factor: 3.241
Abstract
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.
MeSH terms
Aconitate Hydratase; Binding Sites; Candida; Electron Spin Resonance Spectroscopy; Hydro-Lyases; Iron; Protein Binding; Protein Conformation; Spectrum Analysis; Sulfur; Temperature
More resources
EndNote: Download