FEBS Letters | |
Mössbauer studies of Escherichia coli biotin synthase: evidence for reversible interconversion between [2Fe‐2S]2+ and [4Fe‐4S]2+ clusters | |
Trautwein, A.X2  Benda, R2  Florentin, D1  Marquet, A1  Tse Sum Bui, B1  | |
[1] Laboratoire de Chimie Organique et Biologique, Université Paris VI – CNRS UMR 7613, 4 place Jussieu, 75252 Paris Cedex 05, France;Institut für Physik, Medizinische Universität, Ratzeburger Allee 160, 23538 Lübeck, Germany | |
关键词: Biotin synthase; Iron-sulfur cluster; Mössbauer spectroscopy; Fe-S; iron-sulphur cluster; AdoMet; S-adenosylmethionine; PFL; pyruvate formate lysate; ARNR; anaerobic ribonucleotide reductase; LAM; lysine 2; 3-aminomutase; EPR; electron paramagnetic resonance; VTMCD; variable-temperature magnetic circular dichroism; DTT; dithiothreitol; FNR; fumarate nitrate reduction; | |
DOI : 10.1016/S0014-5793(99)01300-9 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
The nature and properties of the iron-sulphur (Fe-S) cluster in as-prepared and reduced biotin synthase of Escherichia coli have been investigated by Mössbauer spectroscopy. Our data clearly demonstrate that in the as-prepared sample, the cluster is present as [2Fe-2S]2+ with isomer shift, δ=0.29 mm/s and quadrupole splitting, ΔE Q=0.53 mm/s, indicating incomplete cysteinyl-S coordination. Anaerobic reduction by dithionite in the presence of 55% (v/v) glycerol converts this form to [4Fe-4S]2+ (δ=0.45 mm/s and ΔE Q=1.11 mm/s) and is accompanied by some destruction to Fe2+. This cluster conversion is reversible and when exposed to air, the [4Fe-4S]2+ cluster is quantitatively reconverted to the [2Fe-2S]2+ cluster without any further cluster degradation.
【 授权许可】
Unknown
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