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Issue 9, 2017
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Interdomain flip-flop motion visualized in flavocytochrome cellobiose dehydrogenase using high-speed atomic force microscopy during catalysis

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Abstract

Cellobiose dehydrogenase (CDH) is a dual domain flavocytochrome, which consists of a dehydrogenase (DH) domain containing a flavin adenine dinucleotide and a cytochrome (CYT) domain containing b-type heme. To directly visualize the dynamic domain motion of class-I CDH from Phanerochaete chrysosporium (PcCDH) during catalysis using high-speed atomic force microscopy, the apo-form of PcCDH was anchored to a heme-immobilized flat gold surface that can specifically fix the orientation of the CYT domain. The two domains of CDH are found to be immobile in the absence of cellobiose, whereas the addition of cellobiose triggers an interdomain flip-flop motion involving domain–domain association and dissociation. Our results indicate that dynamic motion of a dual domain enzyme during catalysis induces efficient electron transfer to an external electron acceptor.

Graphical abstract: Interdomain flip-flop motion visualized in flavocytochrome cellobiose dehydrogenase using high-speed atomic force microscopy during catalysis

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Publication details

The article was received on 14 Apr 2017, accepted on 15 Jul 2017 and first published on 03 Aug 2017


Article type: Edge Article
DOI: 10.1039/C7SC01672G
Citation: Chem. Sci., 2017,8, 6561-6565
  • Open access: Creative Commons BY license
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    Interdomain flip-flop motion visualized in flavocytochrome cellobiose dehydrogenase using high-speed atomic force microscopy during catalysis

    H. Harada, A. Onoda, T. Uchihashi, H. Watanabe, N. Sunagawa, M. Samejima, K. Igarashi and T. Hayashi, Chem. Sci., 2017, 8, 6561
    DOI: 10.1039/C7SC01672G

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