A Novel Nitrite Reductase from <i>Acinetobacter haemolyticus</i> for Efficient Degradation of Nitrite
Nitrite reductases play a crucial role in the nitrogen cycle, demonstrating significant potential for applications in the food industry and environmental remediation, particularly for nitrite degradation and detection. In this study, we identified a novel nitrite reductase (<i>Ah</i>NiR)...
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2025-01-01
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| author | Xiao-Yan Yin Emmanuel Mintah Bonku Jian-Feng Yuan Zhong-Hua Yang |
| author_facet | Xiao-Yan Yin Emmanuel Mintah Bonku Jian-Feng Yuan Zhong-Hua Yang |
| author_sort | Xiao-Yan Yin |
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| description | Nitrite reductases play a crucial role in the nitrogen cycle, demonstrating significant potential for applications in the food industry and environmental remediation, particularly for nitrite degradation and detection. In this study, we identified a novel nitrite reductase (<i>Ah</i>NiR) from a newly isolated denitrifying bacterium, <i>Acinetobacter haemolyticus</i> YD01. We constructed a heterologous expression system using <i>E. coli</i> BL21/pET28a-<i>Ah</i>Nir, which exhibited remarkable nitrite reductase enzyme activity of 29 U/mL in the culture broth, substantially higher than that reported for other strains. Structural analysis of <i>Ah</i>NiR revealed the presence of [Fe-S] clusters, with molecular docking studies identifying Tyr-282 and Ala-289 as key catalytic sites. The enzymatic properties of <i>Ah</i>NiR demonstrated an optimal pH of 7.5 and an optimal catalytic temperature of 30 °C. Its kinetic parameters, K<sub>m</sub> and <i>v</i><sub>max,</sub> were 1.53 mmol/L and 10.18 mmol/min, respectively, fitting with the Michaelis–Menten equation. This study represents the first report of a nitrite reductase from a denitrifying bacterium, providing a new enzyme source for nitrite degradation applications in the food industry and environmental remediation, as well as for biosensing technologies aimed at nitrite detection. |
| format | Article |
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| institution | Kabale University |
| issn | 2218-273X |
| language | English |
| publishDate | 2025-01-01 |
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| spelling | doaj-art-e9396d4f4d7c4d08a10ba7725a2e24092025-01-24T13:25:02ZengMDPI AGBiomolecules2218-273X2025-01-011516310.3390/biom15010063A Novel Nitrite Reductase from <i>Acinetobacter haemolyticus</i> for Efficient Degradation of NitriteXiao-Yan Yin0Emmanuel Mintah Bonku1Jian-Feng Yuan2Zhong-Hua Yang3Xingzhi College, Zhejiang Normal University, Jinhua 321100, ChinaState Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, ChinaXingzhi College, Zhejiang Normal University, Jinhua 321100, ChinaXingzhi College, Zhejiang Normal University, Jinhua 321100, ChinaNitrite reductases play a crucial role in the nitrogen cycle, demonstrating significant potential for applications in the food industry and environmental remediation, particularly for nitrite degradation and detection. In this study, we identified a novel nitrite reductase (<i>Ah</i>NiR) from a newly isolated denitrifying bacterium, <i>Acinetobacter haemolyticus</i> YD01. We constructed a heterologous expression system using <i>E. coli</i> BL21/pET28a-<i>Ah</i>Nir, which exhibited remarkable nitrite reductase enzyme activity of 29 U/mL in the culture broth, substantially higher than that reported for other strains. Structural analysis of <i>Ah</i>NiR revealed the presence of [Fe-S] clusters, with molecular docking studies identifying Tyr-282 and Ala-289 as key catalytic sites. The enzymatic properties of <i>Ah</i>NiR demonstrated an optimal pH of 7.5 and an optimal catalytic temperature of 30 °C. Its kinetic parameters, K<sub>m</sub> and <i>v</i><sub>max,</sub> were 1.53 mmol/L and 10.18 mmol/min, respectively, fitting with the Michaelis–Menten equation. This study represents the first report of a nitrite reductase from a denitrifying bacterium, providing a new enzyme source for nitrite degradation applications in the food industry and environmental remediation, as well as for biosensing technologies aimed at nitrite detection.https://www.mdpi.com/2218-273X/15/1/63nitrite reductase<i>Acinetobacter haemolyticus</i>nitrite reductionhomology modeling |
| spellingShingle | Xiao-Yan Yin Emmanuel Mintah Bonku Jian-Feng Yuan Zhong-Hua Yang A Novel Nitrite Reductase from <i>Acinetobacter haemolyticus</i> for Efficient Degradation of Nitrite Biomolecules nitrite reductase <i>Acinetobacter haemolyticus</i> nitrite reduction homology modeling |
| title | A Novel Nitrite Reductase from <i>Acinetobacter haemolyticus</i> for Efficient Degradation of Nitrite |
| title_full | A Novel Nitrite Reductase from <i>Acinetobacter haemolyticus</i> for Efficient Degradation of Nitrite |
| title_fullStr | A Novel Nitrite Reductase from <i>Acinetobacter haemolyticus</i> for Efficient Degradation of Nitrite |
| title_full_unstemmed | A Novel Nitrite Reductase from <i>Acinetobacter haemolyticus</i> for Efficient Degradation of Nitrite |
| title_short | A Novel Nitrite Reductase from <i>Acinetobacter haemolyticus</i> for Efficient Degradation of Nitrite |
| title_sort | novel nitrite reductase from i acinetobacter haemolyticus i for efficient degradation of nitrite |
| topic | nitrite reductase <i>Acinetobacter haemolyticus</i> nitrite reduction homology modeling |
| url | https://www.mdpi.com/2218-273X/15/1/63 |
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