Interdomain electron transfer in cellobiose dehydrogenase is governed by surface electrostatics

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• 作者：Alan Kadek^a ; ^b ; Daniel Kavan^a ; ^b ; Julien Marcoux^c ; ^d ; ¹ ; Johann Stojko^c ; ^d ; Alfons K.G. Felice^e ; Sarah Cianfé ; rani^c ; ^d ; Roland Ludwig^e ; Petr Halada^a ; Petr Man^a ; ^b ; ^{pman@biomed.cas.cz}
• 关键词：CDH ; cellobiose dehydrogenase ; DH ; dehydrogenase (domain) ; CYT ; cytochrome (domain) ; HDX-MS ; hydrogen/deuterium exchange mass spectrometry ; IET ; interdomain electron transfer ; IM-MS ; ion mobility mass spectrometry
• 刊名：Biochimica et Biophysica Acta (BBA) - General Subjects
• 出版年：2017
• 出版时间：February 2017
• 年：2017
• 卷：1861
• 期：2
• 页码：157-167
• 全文大小：2900 K
• 卷排序：1861

文摘

Cellobiose dehydrogenase and its interdomain interaction were studied in solution. CDH is extensively O-glycosylated in the linker region. H/D exchange was used to describe structure changes in CDH at different pH values. Ion mobility points at higher electrostatic repulsion between domains at neutral pH. Charge neutralization at acidic pH enables the domain interaction in CDH.