The transcription regulator RcoM-2 from Burkholderia xenovorans is a cysteine-ligated hemoprotein that undergoes a redox-mediated ligand switch.
The transcription regulator RcoM-2 from Burkholderia xenovorans is a cysteine-ligated hemoprotein that undergoes a redox-mediated ligand switch.
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DOI：
10.1021/bi800486x
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发表时间：
2008-08-26
期刊：
影响因子：
2.9
通讯作者：
Burstyn, Judith N.
中科院分区：
文献类型：
--
作者：
Marvin, Katherine A.;Kerby, Robert L.;Youn, Hwan;Roberts, Gary P.;Burstyn, Judith N.
Spectroscopic characterization of the newly discovered heme-PAS domain sensor protein BxRcoM-2 reveals that this protein undergoes redox-dependent ligand switching and CO- and NO-induced ligand displacement. The aerobic bacterium Burkholderia xenovorans expresses two homologous heme-containing proteins that promote CO-dependent transcription in vivo. These regulators of CO metabolism, BxRcoM-1 and BxRcoM-2, are gas-responsive heme-PAS domain proteins like the mammalian neuronal PAS domain protein 2 (NPAS2) and the direct oxygen sensor from E. coli (EcDos). BxRcoM-2 was studied using electronic absorption, MCD, resonance Raman and EPR spectroscopies. In the Fe(III) oxidation state, the heme is low-spin and 6-coordinate with a cysteine(thiolate) as one of the two ligands. The sixth ligand is a histidine (His74), which is present in all states of the protein studied. Reduction to the Fe(II) oxidation state results in replacement of the cysteine(thiolate) by a neutral thioether ligand, Met104. CO and NO bind to the Fe(II)BxRcoM-2 heme opposite the histidine ligand. Thus, BxRcoM-2 employs similar coordination state changes to those known for CO-sensing CooA, with redox dependent loss of a cysteine(thiolate) ligand and displacement of a relatively weakly bound axial ligand by the effector gas molecule. Like EcDos, the weakly bound axial ligand that is displaced is methionine.
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DOI：
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发表时间：
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影响因子：
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作者：
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影响因子：
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发表时间：
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影响因子：
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