FEBS Letters | |
Identification of the axial heme ligands of cytochrome b 556 in succinate: Ubiquinone oxidoreductase from Escherichia coli | |
Peterson, Jim2  Gennis, Robert B.1  Vibat, Cecile1  | |
[1] School of Chemical Sciences, University of Illinois, 505 South Mathews Street, Urbana, IL 61801, USA;Department of Chemistry, The University of Alabama, Box 870336, Tuscaloosa, AL 35487, USA | |
关键词: Heme protein; Axial ligand; EPR; MCD; Succinate dehydrogenase; EDTA; ethylenediaminetetracetic acid; EPR; electron paramagnetic resonance; HEPES; N-(2-hydroxyethyl)piperazine-N′-(2-ethanesulfonic acid); MCD; magnetic circular dichroism; | |
DOI : 10.1016/0014-5793(94)01189-3 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Electron paramagnetic resonance (EPR) and near-infrared magnetic circular dichroism (MCD) have been used to identify the ligands to the cytochrome b 556 component of succinate: ubiquinone oxidoreductase (succinate dehydrogenase) from Escherichia coli. The ‘highly axial low spin’ (HALS) EPR spectrum suggests bis(histidine) ligation of the heme with the histidines in a staggered configuration. The near-infrared MCD spectrum exhibits a low energy maximum at 1600 nm which is also clearly indicative of bis(histidine) ligation of the heme iron. The data unambiguously demonstrate that the heme b 556 is ligated to E. coli succinate dehydrogenase via two histidines.
【 授权许可】
Unknown
【 预 览 】
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RO201912020300340ZK.pdf | 179KB | download |