Biology subjects

Nuernberg, D. J.

Publications and source records attributed to Nuernberg, D. J..

3 recordsLinked to original sources

bioRxiv2026

Far-Red Light Photoacclimation Rewires Antenna-Photosystem Organization in Cyanobacterial Cells

Thylakoid membrane remodeling regulates photosynthetic activity in response to changing light, but it is unknown whether such membrane-scale control exists in cyanobacteria, which lack the spatially segregated membrane domains of green algae and plants. Using cryo-electron tomography guided by single-cell hyperspectral correlative imaging, we link spectral acclimation state to thylakoid architecture in far-red light adapting cyanobacteria. We determine the native structures of phycobilisome-photosystem II supercomplexes at subnanometer resolution and show that light-dependent molecular changes propagate across scales to restructure the photosynthetic machinery throughout the thylakoids. We further reveal persistent membrane heterogeneity after prolonged far-red light acclimation and identify a low abundance phycobilisome-photosystem I supercomplex in far-red light conditions. Together, our results frame cyanobacterial thylakoids as plastic membranes that remodel antenna-photosystem structure and organization to regulate photosynthesis.

molecular biology↗

bioRxiv2022

Impact of energy limitations on function and resilience in long-wavelength Photosystem II

Photosystem II (PSII) uses the energy from red light to split water and reduce quinone, an energy-demanding process based on chlorophyll a (Chl-a) photochemistry. Two kinds of cyanobacterial PSII can use Chl-d and Chl-f to perform the same reactions using lower energy, far-red light. PSII from Acaryochloris marina has Chl-d replacing all but one of its 35 Chl-a, while PSII from Chroococcidiopsis thermalis, a facultative far-red species, has just 4 Chl-f and 1 Chl-d and 30 Chl-a. From bioenergetic considerations, the far-red PSII were predicted to lose photochemical efficiency and/or resilience to photodamage. Here, we compare enzyme turnover efficiency, forward electron transfer, back-reactions and photodamage in Chl-f-PSII, Chl-d-PSII and Chl-a-PSII. We show that: i) all types of PSII have a comparable efficiency in enzyme turnover; ii) the modified energy gaps on the acceptor side of Chl-d-PSII favor recombination via PD1+Phe- repopulation, leading to increased singlet oxygen production and greater sensitivity to high-light damage compared to Chl-a-PSII and Chl-f-PSII; ii) the acceptor-side energy gaps in Chl-f-PSII are tuned to avoid harmful back reactions, favoring resilience to photodamage over efficiency of light usage. The results are explained by the differences in the redox tuning of the electron transfer cofactors Phe and QA and in the number and layout of the chlorophylls that share the excitation energy with the primary electron donor. PSII has adapted to lower energy in two distinct ways, each appropriate for its specific environment but with different functional penalties.

biochemistry↗

bioRxiv2020

Light-driven formation of high-valent manganese oxide by photosystem II supports evolutionary role in early bioenergetics

Water oxidation and concomitant O2-formation by the Mn4Ca cluster of oxygenic photosynthesis has shaped the biosphere, atmosphere, and geosphere. It has been hypothesized that at an early stage of evolution, before photosynthetic water oxidation became prominent, photosynthetic formation of Mn oxides from dissolved Mn(2+) ions may have played a key role in bioenergetics and possibly facilitated early geological manganese deposits. The biochemical evidence for the ability of photosystems to form extended Mn oxide particles, lacking until now, is provided herein. We tracked the light-driven redox processes in spinach photosystem II (PSII) particles devoid of the Mn4Ca clusters by UV-vis and X-ray spectroscopy. We find that oxidation of aqueous Mn(2+) ions results in PSII-bound Mn(III,IV)-oxide nanoparticles of the birnessite type comprising 50-100 Mn ions per PSII. Having shown that even todays photosystem-II can form birnessite-type oxide particles efficiently, we propose an evolutionary scenario, which involves Mn-oxide production by ancestral photosystems, later followed by down-sizing of protein-bound Mn-oxide nanoparticles to finally yield todays Mn4CaO5 cluster of photosynthetic water oxidation.

biophysics↗