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Dual role of the active site ‘lid’ regions of protochlorophyllide oxidoreductase in photocatalysis and plant development
Author(s) -
Zhang Shaowei,
Godwin Alan R. F.,
Taylor Aoife,
Hardman Samantha J. O.,
Jowitt Thomas A.,
Johannissen Linus O.,
Hay Sam,
Baldock Clair,
Heyes Derren J.,
Scrutton Nigel S.
Publication year - 2021
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.15542
Subject(s) - protochlorophyllide , oligomer , oxidoreductase , histone octamer , paracrystalline , active site , binding site , biochemistry , biophysics , chemistry , biology , crystallography , enzyme , organic chemistry , nucleosome , histone , gene
The structure of light‐dependent protochlorophyllide oxidoreductase (POR) suggests that amino acid residues in highly conserved active site ‘lid’ regions are responsible for POR oligomer formation. This is confirmed by cryo‐EM of POR–NADPH–Chlide complexes and computational modelling. Studies with variant PORs demonstrate that lid residues are also involved in substrate binding and photocatalysis.