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Crystal Structure of Heliorhodopsin

by Lucas Fernandez – World Editor

Author Correction Published: Structural Details of Light-Driven proton Pump heliorhodopsin Confirmed

A correction to a recently published study clarifies and‌ confirms the crystal structure of heliorhodopsin,​ a light-sensitive protein crucial to ⁤understanding microbial⁤ life and potential bio-inspired technologies. The ​updated findings, published by an international team of ⁣researchers, refine the understanding of this proton pumpS mechanism and offer a more ‍precise blueprint for future investigations.

Heliorhodopsin, discovered in 2017 in the haloarchaeon Halorubrum lacusprofundi, functions as a light-driven proton pump, converting light​ energy into an electrochemical gradient. This process is essential to ⁢energy production in many ⁤microorganisms and has sparked interest in its potential applications in areas like solar energy conversion and optogenetics.​ The initial structural determination faced challenges due to the ​protein’s⁤ inherent flexibility and ​the difficulty in​ obtaining high-quality crystals. ‌This author correction addresses those challenges, providing a more ​robust⁤ and accurate structural model.

The⁤ research⁢ team ‍included Yoshizumi, Kota ⁤Katayama, Satoshi P. Tsunoda, and Hideki ⁤kandori from the Department of Physics, nagoya University and OptoBioTechnology Research Center, Nagoya Institute of ⁣Technology. Additional contributors where Keiichi Inoue (The Institute for Solid State Physics, The University of Tokyo,⁢ PRESTO, Japan Science ​and Technology Agency), Yuji Furutani (Department of ‌Life and Coordination-Complex Molecular Science, Institute for Molecular Science, National Institutes of Natural Sciences, and Department of Structural Molecular Science, The Graduate University for Advanced⁤ Studies⁣ (SOKENDAI)),​ Keitaro⁣ Yamashita (RIKEN SPring-8 Center), Kento Ikeda (School of Mathematical and Physical ⁣Sciences, ⁣Graduate School of Natural Science &⁢ Technology, Kanazawa University), Mikihiro Shibata (Nano Life Science Institute (WPI-NanoLSI),⁢ Kanazawa⁢ University, and High-speed AFM for Biological Application Unit, Institute for Frontier Science Initiative, Kanazawa University), Alina Pushkarev and Oded Béjà (Faculty of Biology, ⁣Technion-Israel Institute of Technology), and Takayuki ‌Uchihashi (Department of Physics, Nagoya University ⁤and Exploratory⁢ Research Center on Life and Living Systems (ExCELLS), National‍ Institutes of ‍Natural Sciences).

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