The Heme Cavity Is Essential for the Peroxidase and Antibacterial Activity of Homodimer Hemoglobin from the Blood Clam Tegillarca granosa.

Autor: Pu, Lili, Dai, Shuting, Wu, Zongming, Wang, Sufang, Bao, Yongbo
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Zdroj: Fishes (MDPI AG); Dec2024, Vol. 9 Issue 12, p512, 10p
Abstrakt: This study investigates the essential role of the heme cavity in the peroxidase and antibacterial activities of homodimeric hemoglobin (Tg-HbI) from the blood clam Tegillarca granosa. After treatment with sodium dodecyl sulfate (SDS), the peroxidase and antibacterial activities of the Tg-HbI were significantly inhibited, with the degree of inhibition correlating positively with the SDS concentration. Fluorescence spectroscopy, UV-Vis spectroscopy, and molecular docking analysis further revealed that SDS interacts with key amino acid residues (e.g., His70 and His102) in the heme cavity of Tg-HbI, causing conformational changes that disrupt the internal hydrophobic interactions, thus inhibiting its function. This study confirms that the antibacterial effect of Tg-HbI is mediated through its peroxidase activity and that the heme cavity plays a critical role in maintaining this activity. These findings lay a foundation for further research on the immune defense functions of hemoglobin and provide new insights into the mechanisms of environmental adaptation in T. granosa. [ABSTRACT FROM AUTHOR]
Databáze: Complementary Index
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