Fig. 4: Ssr1698 catalyzes the reaction of c-type heme to biliverdin IXα. | Communications Biology

Fig. 4: Ssr1698 catalyzes the reaction of c-type heme to biliverdin IXα.

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

Fig. 4

a The degradation assay of MP-11 (c-type heme) with Ssr1698. The decline in the characteristic Soret peak of heme at 408 nm and its shoulder peaks between 500 nm and 600 nm indicates that Ssr1698 degraded the c-type heme, a substrate for Ssr1698. b–e HPLC (b), MS spectra (c, d) and ferrozine assay (e) data indicate the presence of a biliverdin IXα molecule, 11-amino acid peptide and free iron in the reaction product catalyzed by Ssr1698 (cHO) for 2 h and not for 0 h. Error bars indicate the standard deviations of three independent replicates (n = 3). f An equation for the reaction of c-type heme to biliverdin IXα catalyzed by cHO.

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