Time‐resolved fluorescence studies on the dihydrolipoyl transacetylase (E2) component of the pyruvate dehydrogenase complex from Azotobacter vinelandii

FEBS Letters

de Kok, Arie¹  Visser, Antonie J.W.G.¹  Hanemaaijer, Roeland¹  Veeger, Cees¹  Masurel, Remco¹ 

[1] Department of Biochemistry, Agricultural University Dreijenlaan 3,6703 HA Wageningen, The Netherlands

关键词: Dihydrolipoyl transacetylase;    Pyruvate dehydrogenase complex;    Time-resolved fluorescence;    Mobility;    (Azotobacter vinelandii);   

DOI  :  10.1016/0014-5793(88)80498-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The dihydrolipoyl transacetylase (E₂) component of A. vinelandii PDC and its lipoyl domain shows similar dynamic properties as revealed with fluorescence anisotropy decay of lipoyl-bound IAANS. The lipoyl domain (32.6 kDa), containing three almost identical subdomains shows a mode of rotation characteristic for a protein of about 30 kDa. A similar rotation is found in E₂, indicating an independent rotational mobility of the whole domain in the multimeric E₂ core (1.6MDa). No independent rotation of a single lipoyl subdomain (10 kDa) is observed. The E₁ component, in contrast to the E₃ component, shows interaction with the lipoyl domain.

【 授权许可】

Unknown