Abstract
| Original language | English |
|---|---|
| Pages (from-to) | 6561-6565 |
| Number of pages | 5 |
| Journal | Chemical Science |
| Volume | 8 |
| Issue number | 9 |
| DOIs | |
| Publication status | Published - 1 Sep 2017 |
| MoE publication type | A1 Journal article-refereed |
Fingerprint
Cite this
}
Interdomain flip-flop motion visualized in flavocytochrome cellobiose dehydrogenase using high-speed atomic force microscopy during catalysis. / Harada, Hirofumi; Onoda, Akira; Uchihashi, Takayuki; Watanabe, Hiroki; Sunagawa, Naoki; Samejima, Masahiro; Igarashi, Kiyohiki; Hayashi, Takashi.
In: Chemical Science, Vol. 8, No. 9, 01.09.2017, p. 6561-6565.Research output: Contribution to journal › Article › Scientific › peer-review
TY - JOUR
T1 - Interdomain flip-flop motion visualized in flavocytochrome cellobiose dehydrogenase using high-speed atomic force microscopy during catalysis
AU - Harada, Hirofumi
AU - Onoda, Akira
AU - Uchihashi, Takayuki
AU - Watanabe, Hiroki
AU - Sunagawa, Naoki
AU - Samejima, Masahiro
AU - Igarashi, Kiyohiki
AU - Hayashi, Takashi
PY - 2017/9/1
Y1 - 2017/9/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=85027993264&partnerID=8YFLogxK
U2 - 10.1039/c7sc01672g
DO - 10.1039/c7sc01672g
M3 - Article
VL - 8
SP - 6561
EP - 6565
JO - Chemical Science
JF - Chemical Science
SN - 2041-6520
IS - 9
ER -