Abstract Photosynthesis is fundamental for plant growth and yield. The Cytochrome b 6 f complex catalyses a rate-limiting step in thylakoid electron transport and therefore represents an important point of regulation of photosynthesis. Here we show that overexpression of a single core subunit of Cytochrome b 6 f , the Rieske FeS protein, led to up to a 40% increase in the abundance of the complex in Nicotiana tabacum (tobacco) and was accompanied by an enhanced in vitro Cytochrome f activity, indicating a full functionality of the complex. Analysis of transgenic plants overexpressing Rieske FeS by the light-induced fluorescence transients technique revealed a more oxidised primary quinone acceptor of Photosystem II (Q A ) and plastoquinone pool and a faster electron transport from the plastoquinone pool to Photosystem I upon changes in irradiance, compared to control plants. A faster establishing of q E , the energy-dependent component of non-photochemical quenching, in transgenic plants suggested a more rapid build-up of the transmembrane proton gradient, also supporting the increased in vivo Cytochrome b 6 f activity. However, there was no consistent increase in steady-state rates of electron transport or CO 2 assimilation in plants overexpressing Rieske FeS grown in either laboratory conditions or in field trials, suggesting that the in vivo activity of the complex was only transiently increased upon changes in irradiance. Our results show that overexpression of Rieske FeS in tobacco enhances abundance of functional Cytochrome b 6 f and electron transport capacity and may have a potential to increase plant productivity if combined with other traits. One-sentence summary Increased abundance of Cytochrome b 6 f complex leads to transient increases in photosynthetic electron transport rate in tobacco.

Rieske FeS overexpression in tobacco provides increased abundance and activity of Cytochromeb6f