Extended Data Fig. 3: Mutant variants influence the ATPase activity of CydDC.
From: Dissecting the conformational complexity and mechanism of a bacterial heme transporter
(a) Total ATPase activities of wild-type, H85AC, and E500QC variants of CydDC show that unspecific background hydrolysis activity is slightly reduced by the histidine to alanine exchange of the characterized heme binding site, and strongly by the Walker B glutamate to glutamine exchange in NBSC. Total ATPase activity of wild-type CydDC in the presence and absence of GSH exemplifies a non-stimulatory effect. Data are presented as mean values ±s.d. (n = 3 assay technical replicates). (b) Heme (50–500 nM) dependent ATP hydrolysis activity of CydDCE500Q determined by malachite green phosphate assay. (c) Heme (50–500 nM) dependent ATP hydrolysis activity of CydDCH85A determined by malachite green phosphatase assay. All presented ATP hydrolysis data are corrected for background activity in the absence of heme. Data are presented as mean values ±s.d. (n = 3 assay technical replicates).
