期刊论文详细信息
FEBS Letters
Characterization of the paramagnetic iron‐containing redox centres of Thiosphaera pantotropha periplasmic nitrate reductase
Ferguson, Stuart J.2  Reilly, Ann1  Berks, Ben C.1  Richardson, David J.1  Breton, Jacques1  Thomson, Andrew J.1 
[1] Centre for Metalloprotein Spectroscopy and Biology, Schools of Biological and Chemical Sciences, University of East Anglia, Norwich, NR4 7TJ, UK;Department of Biochemistry, University of Oxford, Oxford, OX1 3QU, UK
关键词: Periplasmic nitrate reductase;    Iron—sulphur protein;    cytochrome c-type;    Thiosphaera pantotropha;    EPR;    electron paramagnetic resonance;    MGD;    molybdopterin guanine dinucleotide;   
DOI  :  10.1016/0014-5793(94)00445-5
学科分类:生物化学/生物物理
来源: John Wiley & Sons Ltd.
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【 摘 要 】

Electron paramagnetic resonance spectroscopy signals attributable to low-spin haem c in the oxidised protein and [4Fe–4S]1+ in the dithionite-reduced protein were identified, at low temperature, in Thiosphaera pantotropha periplasmic nitrate reductase. Spin integration of these signals as well as elemental analysis suggest a stoichiometry of 1.3–1.6 c-haem and 1 [4Fe–4S] cluster per enzyme molecule. The E m (at pH 7.4) of the [4F–4S]2+,1+ couple, −160 mV, means that it is unlikely to be physiologically reducible. Peptide sequences from the 90 kDa subunit indicate that the enzyme is a member of the family of molybdopterin guanine dinucleotide-binding polypeptides, the majority of which possess a putative [4Fe–4S] cluster binding sequence and thus may also bind a (low potential) iron—sulphur cluster.

【 授权许可】

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