Hemoglobins Likely Function as Peroxidase in Blood Clam Tegillarca granosa Hemocytes
Hemoglobins are a group of respiratory proteins principally functioning in transport of oxygen and carbon dioxide in red blood cells of all vertebrates and some invertebrates. The blood clam T. granosa is one of the few invertebrates that have hemoglobin-containing red hemocytes. In the present rese...
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| Format: | Article |
| Language: | English |
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Wiley
2017-01-01
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| Series: | Journal of Immunology Research |
| Online Access: | http://dx.doi.org/10.1155/2017/7125084 |
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| author | Sufang Wang Xiaopei Yu Zhihua Lin Shunqin Zhang Liangyi Xue Qinggang Xue Yongbo Bao |
| author_facet | Sufang Wang Xiaopei Yu Zhihua Lin Shunqin Zhang Liangyi Xue Qinggang Xue Yongbo Bao |
| author_sort | Sufang Wang |
| collection | DOAJ |
| description | Hemoglobins are a group of respiratory proteins principally functioning in transport of oxygen and carbon dioxide in red blood cells of all vertebrates and some invertebrates. The blood clam T. granosa is one of the few invertebrates that have hemoglobin-containing red hemocytes. In the present research, the peroxidase activity of T. granosa hemoglobins (Tg-Hbs) was characterized and the associated mechanism of action was deciphered via structural comparison with other known peroxidases. We detected that purified Tg-Hbs catalyzed the oxidation of phenolic compounds in the presence of exogenous H2O2. Tg-Hbs peroxidase activity reached the maximum at pH 5 and 35°C and was inhibited by Fe2+, Cu2+, SDS, urea, and sodium azide. Tg-Hbs shared few similarities in amino acid sequence and overall structural characteristics with known peroxidases. However, the predicted structure at their heme pocket was highly similar to that of horseradish peroxidase (HRP) and myeloperoxidase (MPO). This research represented the first systemic characterization of hemoglobin as a peroxidase. |
| format | Article |
| id | doaj-art-ddea445847334f3fb1adf017a450c26d |
| institution | Kabale University |
| issn | 2314-8861 2314-7156 |
| language | English |
| publishDate | 2017-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | Journal of Immunology Research |
| spelling | doaj-art-ddea445847334f3fb1adf017a450c26d2025-02-03T05:47:16ZengWileyJournal of Immunology Research2314-88612314-71562017-01-01201710.1155/2017/71250847125084Hemoglobins Likely Function as Peroxidase in Blood Clam Tegillarca granosa HemocytesSufang Wang0Xiaopei Yu1Zhihua Lin2Shunqin Zhang3Liangyi Xue4Qinggang Xue5Yongbo Bao6School of Marine Sciences, Ningbo University, Ningbo 315211, ChinaZhejiang Key Laboratory of Aquatic Germplasm Resources, Zhejiang Wanli University, Ningbo 315100, ChinaZhejiang Key Laboratory of Aquatic Germplasm Resources, Zhejiang Wanli University, Ningbo 315100, ChinaZhejiang Key Laboratory of Aquatic Germplasm Resources, Zhejiang Wanli University, Ningbo 315100, ChinaSchool of Marine Sciences, Ningbo University, Ningbo 315211, ChinaZhejiang Key Laboratory of Aquatic Germplasm Resources, Zhejiang Wanli University, Ningbo 315100, ChinaZhejiang Key Laboratory of Aquatic Germplasm Resources, Zhejiang Wanli University, Ningbo 315100, ChinaHemoglobins are a group of respiratory proteins principally functioning in transport of oxygen and carbon dioxide in red blood cells of all vertebrates and some invertebrates. The blood clam T. granosa is one of the few invertebrates that have hemoglobin-containing red hemocytes. In the present research, the peroxidase activity of T. granosa hemoglobins (Tg-Hbs) was characterized and the associated mechanism of action was deciphered via structural comparison with other known peroxidases. We detected that purified Tg-Hbs catalyzed the oxidation of phenolic compounds in the presence of exogenous H2O2. Tg-Hbs peroxidase activity reached the maximum at pH 5 and 35°C and was inhibited by Fe2+, Cu2+, SDS, urea, and sodium azide. Tg-Hbs shared few similarities in amino acid sequence and overall structural characteristics with known peroxidases. However, the predicted structure at their heme pocket was highly similar to that of horseradish peroxidase (HRP) and myeloperoxidase (MPO). This research represented the first systemic characterization of hemoglobin as a peroxidase.http://dx.doi.org/10.1155/2017/7125084 |
| spellingShingle | Sufang Wang Xiaopei Yu Zhihua Lin Shunqin Zhang Liangyi Xue Qinggang Xue Yongbo Bao Hemoglobins Likely Function as Peroxidase in Blood Clam Tegillarca granosa Hemocytes Journal of Immunology Research |
| title | Hemoglobins Likely Function as Peroxidase in Blood Clam Tegillarca granosa Hemocytes |
| title_full | Hemoglobins Likely Function as Peroxidase in Blood Clam Tegillarca granosa Hemocytes |
| title_fullStr | Hemoglobins Likely Function as Peroxidase in Blood Clam Tegillarca granosa Hemocytes |
| title_full_unstemmed | Hemoglobins Likely Function as Peroxidase in Blood Clam Tegillarca granosa Hemocytes |
| title_short | Hemoglobins Likely Function as Peroxidase in Blood Clam Tegillarca granosa Hemocytes |
| title_sort | hemoglobins likely function as peroxidase in blood clam tegillarca granosa hemocytes |
| url | http://dx.doi.org/10.1155/2017/7125084 |
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