title: Time-resolved fluorescence studies on the dihydrolipoyl transacetylase (E2) component of the pyruvate dehydrogenase complex from Azotobacter vinelandii.
abstract: 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 (1.6 MDa). 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.
authors.affiliation: Department of Biochemistry, Agricultural University, Wageningen, The Netherlands.
authors.forename: R
authors.initials: R
authors.lastname: Hanemaaijer
authors.forename: R
authors.initials: R
authors.lastname: Masurel
authors.forename: A J
authors.initials: AJ
authors.lastname: Visser
authors.forename: A
authors.initials: A
authors.lastname: de Kok
authors.forename: C
authors.initials: C
authors.lastname: Veeger
mesh_terms: D000123:Acetyltransferases; D001395:Azotobacter / Q000201:enzymology*; D051047:Dihydrolipoyllysine-Residue Acetyltransferase; D005454:Fluorescence Polarization; D005456:Fluorescent Dyes; D009282:Naphthalenesulfonates; D011768:Pyruvate Dehydrogenase Complex
chemical_list: D005456:Fluorescent Dyes; D009282:Naphthalenesulfonates; D011768:Pyruvate Dehydrogenase Complex; C011488:IAANS; D000123:Acetyltransferases; D051047:Dihydrolipoyllysine-Residue Acetyltransferase