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. Author manuscript; available in PMC: 2015 Oct 1.
Published in final edited form as: Mol Microbiol. 2014 Sep 1;94(1):156–171. doi: 10.1111/mmi.12753

Fig. 6.

Fig. 6

6,8-dichlorooctanoate is attached to all substrates independent of redox environment.

(A) 6,8-Dichlorooctanoate (6,8-diClO) is a structural analog of reduced lipoate (dihydrolipoate).

(B) Modification of the H-protein by lipoate and 6,8-diClO. LipL1 catalyzes the attachment of lipoate as shown in the α-LA western blot (top panels) and 6,8-diClO as shown in the α-6,8-diClO western blot (bottom panels). The α-LA antibodies and the α-6,8-diClO antiserum show very little cross-reactivity.

(C) Effect of reducing conditions on the enzymatic activity of LipL1 against the H-protein. The H-protein is modified by 6,8-diClO independent of the redox environment.

(D) Effect of reducing conditions on the enzymatic activity of LipL1 + LipL2. BCDHLD and KDHLD are modified by 6,8-diClO independent of the redox environment.