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: | Q8DL32 |
Protein Name: | NAD(P)H-quinone oxidoreductase subunit 1 |
Length: | 372 |
Molecular Weight: | 40547.00 |
Species: | Thermosynechococcus elongatus (strain BP-1) [197221] |
Number of TMSs: | 8 |
Location1 / Topology2 / Orientation3: |
Cellular thylakoid membrane1 / Multi-pass membrane protein2 |
Substrate |
proton |
---|
1: MESGIDLQGQ FISALQSLGL SHDLAKLLWL PLPMLMMLIV ATVGVLVAVW LERKISAAVQ
61: QRIGPEYIGP LGILAPLADG LKLIFKEDVL PANSDRWLFT LGPAVVVIPV FLSYIIVPFG
121: QNLLISNLAM GVFLWIALSS IAPIGLLMAG YASNNKYSLL GGLRAAAQSI SYEIPLALAV
181: LAVAMMSNGL GTVEIVEQQS QYGILSWNVW RQPIGFLVFW IAALAECERL PFDLPEAEEE
241: LVAGYQTEYA GMKFALFYLG AYVNLVLSAL LVSVLYFGGW SFPIPLETIA NLLGVSETNP
301: FLQIAFAVLG ITMTLIKAYF FVFLAILLRW TVPRVRIDQL LDLGWKFLLP VGLVNLLLTA
361: GLKLAFPVAF GG