Grana are not essential for photosynthesis, yet they are ubiquitous in higher plants and in the recently evolved
Charaphyta algae; hence grana role and its need is still an intriguing enigma. This article discusses how the grana provide integrated
and multifaceted functional advantages, by facilitating mechanisms that fine-tune the dynamics of the photosynthetic apparatus,
with particular implications for photosystem II (PSII). This dynamic flexibility of photosynthetic membranes is advantageous
in plants responding to ever-changing environmental conditions, from darkness or limiting light to saturating light and sustained
or intermittent high light. The thylakoid dynamics are brought about by structural and organizational changes at the level
of the overall height and number of granal stacks per chloroplast, molecular dynamics within the membrane itself, the partition
gap between appressed membranes within stacks, the aqueous lumen encased by the continuous thylakoid membrane network, and
even the stroma bathing the thylakoids. The structural and organizational changes of grana stacks in turn are driven by physicochemical
forces, including entropy, at work in the chloroplast. In response to light, attractive van der Waals interactions and screening
of electrostatic repulsion between appressed grana thylakoids across the partition gap and most probably direct protein interactions
across the granal lumen (PSII extrinsic proteins OEEp–OEEp, particularly PsbQ–PsbQ) contribute to the integrity of grana stacks.
We propose that both the light-induced contraction of the partition gap and the granal lumen elicit maximisation of entropy
in the chloroplast stroma, thereby enhancing carbon fixation and chloroplast protein synthesizing capacity. This spatiotemporal
dynamic flexibility in the structure and function of active and inactive PSIIs within grana stacks in higher plant chloroplasts
is vital for the optimization of photosynthesis under a wide range of environmental and developmental conditions.
Keywords Entropy - Grana - Oxygen-evolving proteins - Photosystem II - Thylakoid membranes PsbQ–PsbQ interaction - Thylakoid lumen