The NDH-1 complex in Trichodesmium facilitates electron transfer from NAD(P)H to quinones, coupling this process to proton translocation across membranes. In T. erythraeum, this enzyme is pivotal for:
Respiratory metabolism: Maintaining redox balance and ATP synthesis .
Nitrogen fixation: Regulating intracellular oxygen levels to protect nitrogenase activity, as Trichodesmium lacks heterocysts .
Recombinant ndhL is synthesized in multiple systems:
Host System | Purity | Tag | Source |
---|---|---|---|
E. coli | ≥85% | N-terminal His | |
Yeast/Baculovirus | ≥85% | Unspecified | |
Cell-free expression | ≥85% | None |
Key challenges include maintaining proper folding and solubility, often addressed by optimizing buffer conditions (e.g., Tris-based buffers with glycerol) .
Iron limitation: In T. erythraeum, iron scarcity downregulates nifH (nitrogenase) and photosynthetic genes, indirectly affecting NDH-1 activity .
Oxygen regulation: Computational models propose that NDH-1-mediated Mehler reactions reduce intracellular oxygen, enabling simultaneous carbon and nitrogen fixation .
ELISA assays: Used to quantify ndhL expression in environmental or experimental samples .
Structural studies: Recombinant ndhL aids in elucidating subunit interactions within the NDH-1 complex .
Biotechnology: Potential role in bioengineered systems for hydrogen production or redox-driven processes .
Mechanistic gaps: The precise role of ndhL in oxygen regulation during nitrogen fixation remains unclear .
Thermodynamic optimization: T. erythraeum thrives in warm (20–34°C) oligotrophic waters, but recombinant ndhL stability at elevated temperatures is unstudied .
Translational potential: Leveraging ndhL in synthetic biology for biofuel production or bioremediation requires further exploration .
KEGG: ter:Tery_4495
STRING: 203124.Tery_4495