| Autor: |
Sufang Wang, Xiaopei Yu, Shunqin Zhang, Hongyu Jin, Zhongfa Chen, Zhihua Lin, Yongbo Bao |
| Jazyk: |
angličtina |
| Rok vydání: |
2021 |
| Předmět: |
|
| Zdroj: |
Frontiers in Marine Science, Vol 8 (2021) |
| Druh dokumentu: |
article |
| ISSN: |
2296-7745 |
| DOI: |
10.3389/fmars.2021.635210 |
| Popis: |
Beyond its role as an oxygen transport protein, the homodimer hemoglobin of blood clam Tegillarca granosa (Tg-HbI) has been found to possess antibacterial activity. However, the mechanism of antibacterial activity of Tg-HbI remain to be investigated. In this study, we investigated the effects of Cu2+ on the structure, peroxidase activity, and antibacterial ability of Tg-HbI. Tg-HbI was significantly inactivated by Cu2+ in a non-competitive inhibition manner, following first-order reaction kinetics. The Spectroscopy results showed that Cu2+ changed the iron porphyrin ring and the coordination of heme with proximal histidine of Tg-HbI, and increased the hydrophobicity of heme pocket. We found that proline could stabilize the heme pocket structure of Tg-HbI, hence, protect peroxidase activity and antimicrobial activity of Tg-HbI against damage by Cu2+. Our results suggest that Cu2+ inhibits the peroxidase and antibacterial activity of Tg-HbI by destroying its heme pocket structure and Tg-HbI probably plays an antibacterial role through its peroxidase activity. This result could provide insights into the antibacterial mechanism of Tg-HbI. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
|
