The Heme Cavity Is Essential for the Peroxidase and Antibacterial Activity of Homodimer Hemoglobin from the Blood Clam Tegillarca granosa
This study investigates the essential role of the heme cavity in the peroxidase and antibacterial activities of homodimeric hemoglobin (Tg-HbI) from the blood clamTegillarca 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 inT. granosa.
危险品化学品经营许可证（带存储）