Recombinant Synechococcus elongatus NAD(P)H-quinone oxidoreductase subunit 3 (ndhC) is a protein derived from the cyanobacterium Synechococcus elongatus. This protein is part of the NAD(P)H dehydrogenase complex, which plays a crucial role in electron transport chains and photosynthesis. The recombinant form of this protein is often expressed in Escherichia coli (E. coli) for research purposes.
Species: Synechococcus elongatus (strain PCC 7942)
Source: Expressed in E. coli
Tag: Typically His-tagged for purification
Protein Length: Full-length (1-133 amino acids)
Purity: Greater than 90% as determined by SDS-PAGE
Storage: Lyophilized powder stored at -20°C or -80°C
NAD(P)H-quinone oxidoreductase subunit 3 (ndhC) is involved in the electron transport chain, specifically as part of the NAD(P)H dehydrogenase complex. This complex is crucial for transferring electrons from NAD(P)H to quinones, which are essential for generating ATP during photosynthesis and respiration in cyanobacteria.
In cyanobacteria like Synechococcus elongatus, the NAD(P)H dehydrogenase complex contributes to cyclic electron flow around photosystem I (PSI), enhancing ATP synthesis without producing NADPH. This process is vital for balancing the ATP/NADPH ratio required for carbon fixation in the Calvin-Benson-Bassham cycle.
Recombinant ndhC proteins are used in various research applications, including studies on electron transport mechanisms and photosynthetic efficiency. For instance, Synechococcus elongatus has been engineered to produce high levels of heterologous enzymes, demonstrating its potential as a bioreactor for biotechnological applications .
| Characteristics | Description |
|---|---|
| Species | Synechococcus elongatus (strain PCC 7942) |
| Source | Expressed in E. coli |
| Tag | His-tagged |
| Protein Length | Full-length (1-133 amino acids) |
| Purity | Greater than 90% |
| Storage | Lyophilized powder at -20°C or -80°C |
| Amino Acid Sequence | MAKWNSDCSLEFGVFVLNGYEYLLGFLLISSLVPILSLTASRLLRPGRRGPERRTTYESG MEPIGGAWIQFNVRYYMFALVFVIFDVETVFLYPWAVAFNRLGLLAFVEALIFITILVVG LAYAWRKGALEWS |
Cyanobacteria like Synechococcus elongatus are being explored as bioreactors for producing enzymes and other compounds. Their ability to use CO2 and vinasse (a byproduct of ethanol production) as carbon and nitrogen sources makes them attractive for sustainable biotechnology applications .
NDH-1 (NAD(P)H-quinone oxidoreductase) shuttles electrons from an unidentified electron donor, via FMN and iron-sulfur (Fe-S) clusters, to quinones within the respiratory and/or photosynthetic electron transport chain. In this organism, plastoquinone is believed to be the immediate electron acceptor. The enzyme couples this redox reaction to proton translocation, conserving redox energy as a proton gradient. In cyanobacteria, NDH-1 also contributes to inorganic carbon concentration.
KEGG: syf:Synpcc7942_1180
STRING: 1140.Synpcc7942_1180