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It has been recently shown that electron transfer between mitochondrial cytochrome c and the cytochrome c 1 subunit of the cytochrome bc 1 can proceed at long-distance through the aqueous solution. Cytochrome c is thought to adjust its activity by changing the affinity for its partners via Tyr48 phosphorylation, but it is unknown how it impacts the nanoscopic environment, interaction forces, and long-range electron transfer. Here, we constrain the orientation and separation between cytochrome c 1 and cytochrome c or the phosphomimetic Y48 p CMF cytochrome c , and deploy an array of single-molecule, bulk, and computational methods to investigate the molecular mechanism of electron transfer regulation by cytochrome c phosphorylation. We demonstrate that phosphorylation impairs long-range electron transfer, shortens the long-distance charge conduit between the partners, strengthens their interaction, and departs it from equilibrium. These results unveil a nanoscopic view of the interaction between redox protein partners in electron transport chains and its mechanisms of regulation. Electron transfer between mitochondrial cytochrome c and subunit of cytochrome bc 1 can proceed at long distance. Here the authors investigate further the mechanism and show phosphorylation regulation of the interactions between the protein partners in the electron transport chain.

t has been recently shown that electron transfer between mitochondrial cytochrome c and the cytochrome c1 subunit of the cytochrome bc1 can proceed at long-distance through the aqueous solution. Cytochrome c is thought to adjust its activity by changing the affinity for its partners via Tyr48 phosphorylation, but it is unknown how it impacts the nanoscopic environment, interaction forces, and long-range electron transfer. Here, we constrain the orientation and separation between cytochrome c1 and cytochrome c or the phosphomimetic Y48pCMF cytochrome c, and deploy an array of single-molecule, bulk, and computational methods to investigate the molecular mechanism of electron transfer regulation by cytochrome c phosphorylation. We demonstrate that phosphorylation impairs long-range electron transfer, shortens the long-distance charge conduit between the partners, strengthens their interaction, and departs it from equilibrium. These results unveil a nanoscopic view of the interaction between redox protein partners in electron transport chains and its mechanisms of regulation.

Programming rapid, repeatable motions in soft materials has remained a challenge in active matter and biomimetic design. Here, we present a light-controlled chemomechanical network based on Tetrahymena thermophila calcium-binding protein 2 (Tcb2), a Ca2+-sensitive contractile protein. These networks—driven by Ca2+-triggered structural rearrangements—exhibit dynamic selfassembly, spatiotemporal growth, and contraction rates comparable to actomyosin systems. By coupling light-sensitive chelators for optically triggered Ca2+ release, we achieve precise growth and repeatable mechanical contractility of Tcb2 networks, revealing emergent phenomena such as boundary-localized active regions and density gradient-driven reversals in motion. A coupled reaction-diffusion and elastic model explains these dynamics, highlighting the interplay between chemical network assembly and mechanical response. We further demonstrate active transport of particles via network-mediated forces in vitro and implement reinforcement learning to program seconds-scale spatiotemporal actuation in silico. These results establish a platform for designing responsive active materials with rapid chemomechanical dynamics and tunable optical control, with applications in synthetic cells, sub-cellular force generation, and programmable biomaterials.

Field work is an essential component not just for organismal biology, but also for the expanding umbrella of disciplines which have turned their attention towards living systems. Observing organisms in naturalistic contexts is a critical component of discovery; however, conducting field research can be a massive barrier for scientists who do not have experience working with organisms in a naturalistic context under challenging field conditions. Here we propose 8 critical steps for organizing and executing interdisciplinary curiosity-driven field research, drawing on the insights from The in Situ Jungle Biomechanics Lab (JBL). The JBL program is a field research course that helps early-career scientists gain experience in organizing and conducting interdisciplinary field research. JBL uses a curiosity-driven approach to field science education by encouraging early-career researchers to explore scientific questions in the Peruvian Amazon with a non-prescriptive approach to research output. We achieve an inclusive research space by bringing scientists from across disciplines together, with local communities to collaborate and spark new questions and ideas. To stoke curiosity, the JBL imparts a naturalist tradition set forth by organismal biologists of the 20th century who have extolled the merits of observing the natural world as a form of scientific exploration.