Redox-dependent axial ligand replacement and its functional significance in heme-bound iron regulatory proteins
作者： Mariko Ogura , Ryosuke Endo , Haruto Ishikawa , Yukiko Takeda , Takeshi Uchida
DOI: 10.1016/J.JINORGBIO.2018.01.007
关键词:
摘要: Iron regulatory proteins (IRPs), regulators of iron metabolism in mammalian cells, control the translation involved uptake, storage and utilization by binding to specific iron-responsive element (IRE) sequences mRNAs. Two homologs IRPs (IRP1 IRP2) have a typical heme motif (HRM), consensus sequence found "heme-regulated proteins". However, HRM has been reported only for IRP2, which is essential oxidative modification loss target In this paper, we confirmed that IRP1 also specifically binds two molar equivalents heme, absorption resonance Raman spectra heme-bound were quite similar those IRP2. This shows environmental structures are close using as molecule. Pulse radiolysis experiments, however, clearly revealed an axial ligand exchange from Cys His immediately after reduction form 5-coordinate His-ligated whereas was not observed IRP1. Considering but IRP1, probably owing structural flexibility propose transient prerequisite functionally differentiates IRP2
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