| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | nosZ |
| Uniprot No | Q51705 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 58-553aa |
| 氨基酸序列 | ASGDGSVAPGQLDDYYGFWSSGQSGEMRILGIPSMRELMRVPVFNRCSATGWGQTNESVRIHERTMSERTKKFLAANGKRIHDNGDLHHVHMSFTEGKYDGRFLFMNDKANTRVARVRCDVMKCDAILEIPNAKGIHGLRPQKWPRSNYVFCNGEDETPLVNDGTNMEDVANYVNVFTAVDADKWEVAWQVLVSGNLDNCDADYEGKWAFSTSYNSEKGMTLPEMTAAEMDHIVVFNIAEIEKAIAAGDYQELNGVKVVDGRKEASSLFTRYIPIANNPHGCNMAPDKKHLCVAGKLSPTATVLDVTRFDAVFYENADPRSAVVAEPELGLGPLHTAFDGRGNAYTSLFLDSQVVKWNIEDAIRAYAGEKVDPIKDKLDVHYQPGHLKTVMGETLDATNDWLVCLSKFSKDRFLNVGPLKPENDQLIDISGDKMVLVHDGPTFAEPHDAIAVHPSILSDIKSVWDRNDPMWAETRAQAEADGVDIDNWTEEVIRDG |
| 预测分子量 | 71.1 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于nosZ重组蛋白的3篇参考文献示例(文献信息为模拟示例，仅供参考)：
1. **"Heterologous expression and purification of nosZ-encoded nitrous oxide reductase from *Pseudomonas stutzeri*"**
- **作者**: Smith J, et al.
- **摘要**: 研究通过在大肠杆菌中异源表达重组nosZ蛋白，优化纯化条件并获得高纯度酶，验证其催化N2O还原为N2的活性，为酶学机制研究提供基础。
2. **"Crystal structure analysis of recombinant nosZ reveals insights into its catalytic copper centers"**
- **作者**: Tanaka K, et al.
- **摘要**: 解析了重组nosZ蛋白的晶体结构，揭示了其活性位点的铜离子配位构型，阐明了电子传递路径及底物结合的关键残基，为理解反硝化酶功能提供结构依据。
3. **"Functional characterization of nosZ mutants generated by site-directed mutagenesis"**
- **作者**: Müller L, et al.
- **摘要**: 通过定点突变重组nosZ蛋白，发现特定组氨酸和半胱氨酸残基对酶活性至关重要，并证明其氧敏感性对工业应用中的稳定性影响。
**Background of nosZ Recombinant Protein**
The *nosZ* gene encodes nitrous oxide reductase, a key enzyme responsible for the reduction of nitrous oxide (N₂O) to dinitrogen (N₂) during microbial denitrification. This process is critical for closing the nitrogen cycle, as N₂O is a potent greenhouse gas and ozone-depleting compound. Environmental concerns over rising N₂O emissions have driven interest in understanding the structure, function, and regulation of NosZ, particularly in the context of climate change mitigation and sustainable agriculture.
Recombinant NosZ protein is produced by heterologous expression of the *nosZ* gene in model organisms like *E. coli*, enabling large-scale purification and detailed biochemical studies. This approach bypasses challenges associated with cultivating native denitrifying microbes, many of which are fastidious or slow-growing. Recombinant systems allow researchers to explore enzyme kinetics, cofactor requirements (e.g., Cu ions in the active site), and electron transfer mechanisms underpinning N₂O reduction.
Studies on NosZ have revealed genetic and functional diversity across microbial taxa, with two distinct clades (I and II) identified. Clade II NosZ, found in diverse non-denitrifiers, exhibits unique structural features and may play an underappreciated role in environmental N₂O consumption. Engineering or enhancing NosZ activity through recombinant protein studies offers potential applications in bioremediation, biofertilizers, or industrial biocatalysts to mitigate N₂O emissions.
However, challenges remain, including optimizing enzyme stability, understanding interactions with electron donors, and scaling up for real-world implementation. Ongoing research integrates genomics, structural biology, and synthetic biology to unlock the full potential of NosZ in addressing global nitrogen pollution and climate challenges.
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