Acclimation of photosynthesis began with a Cu-binding superoxide detoxifying enzyme

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Abstract

Plant acclimation is a growing scientific concept, at molecular, cellular and global scales. All photosynthetic organisms that created an oxic atmosphere on earth possess a gene of unknown function “ Acclimation of Photosynthesis to the Environment 1 ”. Here we show that APE1 encodes a thylakoid-bound protein with a unique motif that binds copper and detoxifies the superoxide anion radical, O 2 •− . Maturation of the recombinant APE1 protein from Chlamydomonas reinhardtii requires formation of cysteine disulfide bonds after copper binding or via a high affinity interaction with a copper chaperone (Plastid Copper Chaperone 1) that boosts its scavenging capacity for O 2 •− . APE1 co-occurs in evolution with Photosystem II oxygen evolving proteins and it is the archaic O 2 •− detoxifying enzyme for acclimating photosynthesis to an oxygenic environment.
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Abstract Plant acclimation is a growing scientific concept, at molecular, cellular and global scales. All photosynthetic organisms that created an oxic atmosphere on earth possess a gene of unknown function “Acclimation of Photosynthesis to the Environment 1”. Here we show that APE1 encodes a thylakoid-bound protein with a unique motif that binds copper and detoxifies the superoxide anion radical, O2•−. Maturation of the recombinant APE1 protein from Chlamydomonas reinhardtii requires formation of cysteine disulfide bonds after copper binding or via a high affinity interaction with a copper chaperone (Plastid Copper Chaperone 1) that boosts its scavenging capacity for O2•−. APE1 co-occurs in evolution with Photosystem II oxygen evolving proteins and it is the archaic O2•− detoxifying enzyme for acclimating photosynthesis to an oxygenic environment. Competing Interest Statement The authors have declared no competing interest.

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last seen: 2026-05-20T01:45:00.602351+00:00