Beyond monofunctionality: structural perspectives on phenol oxidase side activity in a catalase

Ferousi, C.; Kosinas, C.; Pantelakis, O.I.; Nikolaivits, E.; Topakas, E.; Dimarogona, M.

doi:10.1107/S2059798326009848

Figure 3
(a) Cartoon representation of the tetrameric form of ClCPO. Each monomer is coloured separately. Haem b molecules and other ligands are shown as sticks. (b) Cartoon representation of the ClCPO monomer. Termini of the protein are highlighted along with monomeric regions. (c) Stick representation of the haem b, Tyr357 and a water molecule that were modelled in the 2F_o − F_c map of molecule H of the ClCPO crystallographic structure. The OH group of Tyr357 and a water molecule coordinate the iron ion of the porphyrin ring.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 82| Part 11| November 2026|

https://doi.org/10.1107/S2059798326009848

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