Ruffling is essential for Staphylococcus aureus IsdG-catalyzed degradation of heme to staphylobilin.

ABSTRACT: Non-canonical heme oxygenases are enzymes that degrade heme to non-biliverdin products within bacterial heme iron acquisition pathways. These enzymes all contain a conserved second-sphere Trp residue that is essential for enzymatic turnover. Here, UV/Vis absorption (Abs) and circular dichroism (CD) spectroscopies were employed to show that the W67F variant of IsdG perturbs the heme substrate conformation. In general, a dynamic equilibrium between "planar" and "ruffled" substrate conformations exists within non-canonical heme oxygenases, and that the second-sphere Trp favors population of the "ruffled" substrate conformation. ¹H nuclear magnetic resonance and magnetic CD spectroscopies were used to characterize the electronic structures of IsdG and IsdI variants with different su

SUBMITTER: Schuelke-Sanchez AE 

PROVIDER: S-EPMC8930504 | biostudies-literature | 2022 May

REPOSITORIES: biostudies-literature