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Thylakoid protein vitamin K epoxide reductase ( At VKOR/LTO1) is involved in oxidoreduction. The deficiency of this compound causes pleiotropic defects in  Arabidopsis thaliana , such as severely stunted growth, smaller sized leaves, and delay of flowering. Transgenic complementation of wild-type  At VKOR (VKOR WT ) to  vkor  mutant lines ultimately demonstrates that the phenotype changes are due to this gene. However, whether  At VKOR functions in  Arabidopsis  through its protein oxidoreduction is unknown. To further study the redox-active sites of  At VKOR  in vivo , a series of plasmids containing cysteine-mutant VKORs were constructed and transformed into  vkor  deficient lines. Compared with transgenic  At VKOR WT  plants, the size of the transgenic plants with a single conservative cysteine mutation (VKOR C109A , VKOR C116A , VKOR C195A , and VKOR C198A ) were smaller, and two double-cysteine mutations (VKOR C109AC116A  and VKOR C195AC198A ) showed significantly stunted growth, similar with the  vkor  mutant line. However, mutations of two non-conservative cysteines (VKOR C46A  and VKOR C230A ) displayed little obvious changes in the phenotypes of  Arabidopsis . Consistently, the maximum and actual efficiency of photosystem II (PSII) in double-cysteine mutation plants decreased significantly to the level similar to that of the  vkor  mutant line both under normal growth light and high light. A significantly decreased amount of D1 protein and increased accumulation of reactive oxygen species were observed in two double-cysteine mutations under high light. All of the results above indicated that the conservative cysteines in transmembrane domains were the functional sites of  At VKOR in  Arabidopsis  and that the oxidoreductase activities of  At VKOR were directly related to the autotrophic photosynthetic growth and PSII activity of  Arabidopsis thaliana .

The conservative cysteines in transmembrane domain of AtVKOR/LTO1 are critical for photosynthetic growth and photosystem II activity in Arabidopsis