Patel Stuti N, Sonani Ravi R, Gupta Gagan D, Singh Niraj Kumar, Upadhyaya Chandni, Sonavane Bhargavi, Amin Seema, Kumar Vinay, Madamwar Datta
P. D. Patel Institute of Applied Sciences, Charotar University of Science and Technology, Changa, Anand, Gujarat, India.
Department of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, VA, USA.
FEBS Lett. 2025 May;599(10):1420-1432. doi: 10.1002/1873-3468.70048. Epub 2025 Apr 29.
Phycocyanin (PC), a pigment-protein complex with diverse biotechnological applications, plays a key role in light energy transfer for photosynthesis in cyanobacteria. PC (O-PC) from a thermotolerant cyanobacteria Oscillatoria sp. N09DM exhibits remarkable stability compared to its mesophilic counterparts, making it highly valuable for industrial and medical applications. To understand the basis of its stability, the crystal structure of O-PC is solved and analysed. Structural analysis reveals a key molecular interaction, including hydrogen bonds, salt bridges and hydrophobic interactions, along with amino acid substitutions that provide the thermal stability. Additionally, structural results provide insights into chromophore-protein interactions for understanding O-PC's role in the efficient transfer of light energy.
藻蓝蛋白（PC）是一种具有多种生物技术应用的色素 - 蛋白质复合物，在蓝细菌光合作用的光能传递中起关键作用。来自耐热蓝细菌颤藻属N09DM的PC（O - PC）与其嗜温同类相比具有显著的稳定性，这使其在工业和医学应用中具有很高的价值。为了了解其稳定性的基础，对O - PC的晶体结构进行了解析和分析。结构分析揭示了一种关键的分子相互作用，包括氢键、盐桥和疏水相互作用，以及提供热稳定性的氨基酸取代。此外，结构结果为发色团 - 蛋白质相互作用提供了见解，有助于理解O - PC在光能高效传递中的作用。
