Modeling the Characteristic Residues of Chlorophyll f Synthase (ChlF) from Halomicronema hongdechloris to Determine Its Reaction Mechanism

Abstract

Photosystem II (PSII) is a quinone-utilizing photosynthetic system that converts light energy into chemical energy and catalyzes water splitting. PsbA (D1) and PsbD (D2) are the core subunits of the reaction center that provide most of the ligands to redox-active cofactors and exhibit photooxidoreductase activities that convert quinone and water into quinol and dioxygen. The performed analysis explored the putative uncoupled electron transfer pathways surrounding P680+ induced by far-red light (FRL) based on photosystem II (PSII) complexes containing substituted D1 subunits in Halomicronema hongdechloris. Chlorophyll f-synthase (ChlF) is a D1 protein paralog. Modeling PSII-ChlF complexes determined several key protein motifs of ChlF. The PSII complexes included a dysfunctional Mn4CaO5 cluster where ChlF replaced the D1 protein. We propose the mechanism of chlorophyll f synthesis from chlorophyll a via free radical chemistry in an oxygenated environment created by over-excited pheophytin a and an inactive water splitting reaction owing to an uncoupled Mn4CaO5 cluster in PSII-ChlF complexes. The role of ChlF in the formation of an inactive PSII reaction center is under debate, and putative mechanisms of chlorophyll f biosynthesis are discussed.