AUTHOR=Wang Sufang , Yu Xiaopei , Zhang Shunqin , Jin Hongyu , Chen Zhongfa , Lin Zhihua , Bao Yongbo TITLE=Cu2+ Inhibits the Peroxidase and Antibacterial Activity of Homodimer Hemoglobin From Blood Clam Tegillarca granosa by Destroying Its Heme Pocket Structure JOURNAL=Frontiers in Marine Science VOLUME=8 YEAR=2021 URL=https://www.frontiersin.org/journals/marine-science/articles/10.3389/fmars.2021.635210 DOI=10.3389/fmars.2021.635210 ISSN=2296-7745 ABSTRACT=

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.