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: | Q8DKY0 |
Protein Name: | NAD(P)H-quinone oxidoreductase chain 4 1 |
Length: | 529 |
Molecular Weight: | 57809.00 |
Species: | Thermosynechococcus elongatus (strain BP-1) [197221] |
Number of TMSs: | 14 |
Location1 / Topology2 / Orientation3: |
Cellular thylakoid membrane1 / Multi-pass membrane protein2 |
Substrate |
proton |
---|
1: MSTFPWLTTI ILFPIVAALA IPFIPDPTGK GRPIRWYALA VGLIDFALIV YAFTNFYDLN
61: TPGMQLWESY DWIPEIGLRW SVGADGLSMP LILLTGFITT LAILAAWPVT LKPRLFYFLM
121: LAMYGGQIAV FAVQDMLVFF LAWELELIPV YLLLAIWGGH KRQYAATKFI LYTAGSSLFI
181: LVAGLAMAFY GDTVSFDMQT LAAKDYALGF QLLVYAGFLV AYGVKLPIVP LHTWLPDAHG
241: EATAPVHMLL AGILLKMGGY ALIRMNVDML PAAHAKFAPV LVILGVVNII YAALTSYAQR
301: NLKRKIAYSS ISHIGFVLIG IASFTNLGMS GAVLQMVSHG LIGASLFFLV GATYDRTHTL
361: ILEEMGGVGQ KMKKIFAMFT ACSLASLALP GMSGFVAELM VFIGFATSDA YSLPFRVIVV
421: FLAAVGVILT PIYLLSMLRE IFYGPENKEL VEHEALVDAE PREVFIIACL LVPIIGIGLY
481: PKLLTQIYDA TTGQVIARAR EVLPTLAQQT EQPLGILPMV APQLKANAQ