3.D.1.8.2 The photosynthetic/respiratory NAD(P)H-quinone oxidoreductase subunits A - Q and S. NdhP and NdhQ are peptides of 42 and 39 aas, identified by cryoEM at 3.3 Å resolution (Schuller et al. 2019). NDH-1 (NdhA) shuttles electrons from reduced ferridoxin, via FMN and iron-sulfur (Fe-S) centers, to quinones in
the respiratory and photosynthetic chains. The immediate electron
acceptor for the enzyme in this species is believed to be plastoquinone. The system couples the redox reaction to proton translocation, and thus conserves
the redox energy in a proton gradient (Schuller et al. 2019). Ferridoxin directly mediates electron transfer between photosystem I and complex I. Ferridoxin efficiently binds to complex I with subunit NdhS being the key component in this process (Schuller et al. 2019).
|
Accession Number: | Q8DJD9 |
Protein Name: | NAD(P)H-quinone oxidoreductase subunit H |
Length: | 394 |
Molecular Weight: | 45216.00 |
Species: | Thermosynechococcus elongatus (strain BP-1) [197221] |
Location1 / Topology2 / Orientation3: |
Cellular thylakoid membrane1 / Peripheral membrane protein2 / Cytoplasmic side3 |
Substrate |
proton |
---|
1: MPKIETRTEP MVINMGPHHP SMHGVLRLMV TLDGEDVIDC EPVIGYLHRG MEKIAENRTN
61: IMFIPYVSRW DYAAGMFNEA VTVNAPEKLA GIPVPKRASY IRVIMLELNR IANHLLWLGP
121: FLADVGAQTP FFYIFREREY IYDLFEAATG MRFINNNYFR IGGVAADLTY GWVTKCRDFC
181: DYFLPKVDEY ERLITNNPIF VRRLQGVGKI SREEAINWGL SGPMLRASGV KWDLRKVDHY
241: ECYDDFDWDV PVATEGDCLA RYIVRIQEMR ESVKIIRQAL DGLPGGPYEN LEAKRMLEGA
301: KSEWNGFDYQ YIGKKLSPTF KIPKGEHYVR VESGKGELGI YLIGDDNVFP WRWKIRPPDF
361: NNLQVLPQLL KGMKVADIVA ILGSIDVIMG SVDR