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Catalysis by the non-heme iron(II) histone demethylase PHF8 involves iron center rearrangement and conformational modulation of substrate orientation

Abstract:

PHF8 (KDM7B) is a human non-heme 2-oxoglutarate (2OG) JmjC domain oxygenase that catalyzes the demethylation of the di/mono-Nε-methylated K9 residue of histone H3. Altered PHF8 activity is linked to genetic diseases and cancer; thus, it is an interesting target for epigenetic modulation. We describe the use of combined quantum mechanics/molecular mechanics (QM/MM) and molecular dynamics (MD) simulations to explore the mechanism of PHF8, including dioxygen activation, 2OG binding modes, and su...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1021/acscatal.9b04907

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Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Organic Chemistry
Role:
Author
ORCID:
0000-0002-0290-6565
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Publisher:
American Chemical Society Publisher's website
Journal:
ACS Catalysis Journal website
Volume:
10
Issue:
2
Pages:
1195-1209
Publication date:
2019-12-11
Acceptance date:
2019-12-11
DOI:
EISSN:
2155-5435
Source identifiers:
1077466
Language:
English
Keywords:
Pubs id:
pubs:1077466
UUID:
uuid:38b6bcc4-c030-4e7d-af2d-d2826a206396
Local pid:
pubs:1077466
Deposit date:
2019-12-12

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