Structure and stability of phycocyanin from thermotolerant <i>Oscillatoria</i>

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.

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Publication Details

Journal
FEBS Letters
Published
2025-04-29
DOI
https://doi.org/10.1002/1873-3468.70048
Citations
1
Primary Topic
Photosynthetic Processes and Mechanisms
Type
article
Field-Weighted Citation Impact
0.81

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article

Structure and stability of phycocyanin from thermotolerant Oscillatoria

Vinay Kumar, Niraj Singh, Ravi R. Sonani, Seema Amin et al.
1 citations
FEBS Letters
Photosynthetic Processes and Mechanisms
0.81
article

Structure and stability of phycocyanin from thermotolerant Oscillatoria

Vinay Kumar, Niraj Singh, Ravi R. Sonani, Seema Amin, Stuti Patel, Gagan D. Gupta, Datta Madamwar, Chandni Upadhyaya, Bhargavi Sonavane
article en
1 citations

Abstract

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.

FEBS LettersVol. 599(10)
Bhabha Atomic Research Centre (IN), Government of Gujarat (IN), Charotar University of Science and Technology (IN), University of Virginia (US), Sardar Patel University (IN)
Gujarat Council on Science and Technology
Affordable and clean energy
Openalex Percentile: Top 29%
Photosynthetic Processes and Mechanisms
0.81
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Structure and stability of phycocyanin from thermotolerant <i>Oscillatoria</i> — Vinay Kumar, Niraj Singh, et al. · FEBS Letters (2025) | TGRS Research Map | TGRS