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

Hirofumi Harada, Akira Onoda, Takayuki Uchihashi, Hiroki Watanabe, Naoki Sunagawa, Masahiro Samejima, Kiyohiko Igarashi, Takashi Hayashi

    Research output: Contribution to journalArticleScientificpeer-review

    18 Citations (Scopus)

    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.
    Original languageEnglish
    Pages (from-to)6561-6565
    JournalChemical Science
    Volume8
    Issue number9
    DOIs
    Publication statusPublished - 1 Sep 2017
    MoE publication typeA1 Journal article-refereed

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