The Heme Cavity Is Essential for the Peroxidase and Antibacterial Activity of Homodimer Hemoglobin from the Blood Clam <i>Tegillarca granosa</i>

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 <i>Tegillarca granosa</i>. After treatment with sodium dodecyl sulfate (SDS), the peroxidase and antibacterial activities of...

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Bibliographic Details
Main Authors: Lili Pu, Shuting Dai, Zongming Wu, Sufang Wang, Yongbo Bao
Format: Article
Language:English
Published: MDPI AG 2024-12-01
Series:Fishes
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Online Access:https://www.mdpi.com/2410-3888/9/12/512
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Summary: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 <i>Tegillarca granosa</i>. 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 <i>T. granosa</i>.
ISSN:2410-3888