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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| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
| Published: |
MDPI AG
2025-01-01
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| Series: | Biomolecules |
| Subjects: | |
| Online Access: | https://www.mdpi.com/2218-273X/15/1/63 |
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| Summary: | 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. |
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| ISSN: | 2218-273X |