The molecular mechanism of heme loss from oxidized soluble guanylate cyclase induced by conformational change
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- 作者：Jie Pana ; Xiaoxue Zhanga ; Hong Yuana ; Qiming Xub ; Huijuan Zhanga ; Yajun Zhoua ; Zhong-Xian Huanga ; Xiangshi Tana ; b ; xstan@fudan.edu.cn" class="auth_mail" title="E-mail the corresponding author
- 关键词：sGC ; soluble guanylate cyclase ; NO ; nitric oxide ; FRET ; fluorescence resonance energy transfer ; H-NOX domain ; heme-NO/O2-binding domain ; PAS domain ; Per/Arnt/Sim domain ; CC ; helical domain ; Ns H-NOX ; the H-NOX domain of Nostoc sp ; FlAsH-EDT2 ; fluorescein arsenical helix binder ; GTP ; guanosine 5&prime ; -triphosphate ; cGMP ; 3&prime ; 5&prime ; -cyclic guanosine monophosphate ; DEA/NO ; diethylammonium (Z)-1-(N ; N-diethylamino) diazen-1-ium-1 ; 2-diolate ; EPR ; electron paramagnetic resonance ; ODQ ; 1H-(1
- 刊名：Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
- 出版年：2016
- 出版时间：May 2016
- 年：2016
- 卷：1864
- 期：5
- 页码：488-500
- 全文大小：3338 K
文摘
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A fluorophore FlAsH-EDT2 monitoring protein conformational change is labeled at different domains of sGC β1 by mutagenesis.
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The molecular mechanism of sGC oxidation and loss induced by conformational change is studied based on FRET.
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The synergistic effect of the conformational changes could force the heme pocket open and heme loss.
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The kinetics of heme loss from oxidized sGC is monitored by the heme de-quenching the fluorescence of FlAsH-EDT2.