Zeaxanthin Epoxidase Activity Is Downregulated by Hydrogen Peroxide

Abstract

Abstract The xanthophyll zeaxanthin (Zx) serves important photoprotective functions in chloroplasts and is particularly involved in the dissipation of excess light energy as heat in the antenna of photosystem II (PSII). Zx accumulates under high-light (HL) conditions in thylakoid membranes and is reconverted to violaxanthin by Zx epoxidase (ZEP) in low light or darkness. ZEP activity is completely inhibited under long-lasting HL stress, and the ZEP protein becomes degraded along with the PSII subunit D1 during photoinhibition of PSII. This ZEP inactivation ensures that high levels of Zx are maintained under harsh HL stress. The mechanism of ZEP inactivation is unknown. Here, we investigated ZEP inactivation by reactive oxygen species (ROS) under in vitro conditions. Our results show that ZEP activity is completely inhibited by hydrogen peroxide (H2O2), whereas inhibition by singlet oxygen or superoxide seems rather unlikely. Due to the limited information about the amount of singlet oxygen and superoxide accumulating under the applied experimental conditions, however, a possible inhibition of ZEP activity by these two ROS cannot be generally excluded. Despite this limitation, our data support the hypothesis that the accumulation of ROS, in particular H2O2, might be responsible for HL-induced inactivation of ZEP under in vivo conditions.