Fig. 3: The binding of apo-Ssr1698 with c-type heme. | Communications Biology

Fig. 3: The binding of apo-Ssr1698 with c-type heme.

From: Identification of a c-type heme oxygenase and its function during acclimation of cyanobacteria to nitrogen fluctuations

Fig. 3

a Ssr1698 shares the DUF2470 domain with bacterial HugZ and ChuZ, which are predicted to provide the interacting interface with heme. b The MP-11 (c-type heme) titration of apo-Ssr1698 (10 µM) as monitored by the difference absorption spectra in PBS buffer (pH 7.4) and 20 µM BSA. The positive characteristic absorption peaks indicate the binding of apo-Ssr1698 with c-type heme. c The titration curve observed at 408 nm for apo-Ssr1698 with c-type heme. Error bars indicate the standard deviations of three independent replicates (n = 3). d The oligomerization state of purified tag-less apo-Ssr1698 is determined by CN-PAGE. Enzyme digestion and purification of S1, S2, and S3 are shown in Supplementary Fig. 8. e A structural model represents the binding of apo-Ssr1698 with c-type heme. Apo-Ssr1698 structure was predicted by AlphaFold, and docking of its dimer with c-type heme was predicted by AutoDockVina.

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