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Time‐resolved fluorescence studies on mutants of the dihydrolipoyl transacetylase (E2) component of the pyruvate dehydrogenase complex from Azotobacter vinelandii
Author(s) -
Schulze Egbert,
Westphal Adrie H.,
Berg Axel,
de Kok Arie
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)81047-r
Subject(s) - azotobacter vinelandii , chemistry , dihydrolipoamide dehydrogenase , biophysics , fluorescence , pyruvate dehydrogenase complex , mutant , domain (mathematical analysis) , biochemistry , fluorescence anisotropy , crystallography , enzyme , biology , physics , nitrogenase , mathematical analysis , mathematics , organic chemistry , quantum mechanics , nitrogen fixation , membrane , gene , nitrogen
Fluorescence anisotropy decays were measured for the wild‐type dihydrolipoyl transacetylase (E2) component of pyruvate dehydrogenase complex from Azotobacter vinelandii and E. coli and for E2‐mutants from A. vinelandii in which the alanine‐proline‐rich sequence between the binding domain and the catalytic domain is partially or completely deleted. In both E2‐mutants the rotational mobility of the lipoyl domain and the overall activity after reconstitution of the complex are significantly decreased indicating the important role of the deleted sequence for the movement of the lipoyl domain and the transfer of substrates between the different active sites within the complex.