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: | Q8DMR6 |
Protein Name: | NAD(P)H-quinone oxidoreductase subunit 2 |
Length: | 515 |
Molecular Weight: | 55144.00 |
Species: | Thermosynechococcus elongatus (strain BP-1) [197221] |
Number of TMSs: | 14 |
Location1 / Topology2 / Orientation3: |
Cellular thylakoid membrane1 / Multi-pass membrane protein2 |
Substrate |
proton |
---|
1: MDLVTLAGQL NAGTILPETI LIVTLLVVLL ADLIQGRQAD RWTPYFAIVG LGGAIATMIP
61: LWTQPATISF FGSFISDHLS LFFRGLIALS ALGTILMSIR YVEQTGSSLG EFMTILLTAT
121: VGGMFIAGAQ ELVFIFVALE TLSIASYLLT GYTKRDSRSN EAALKYLLIG AASSAIFLYG
181: SSLLYGLSGG HTQLPAIAQA LSSESLGLVV ALVFVIAGIS FKISAVPFHQ WTPDVYEGAP
241: TPVVAFLSVG SKAAGFALAI RFLTLAFPSV TDQWQLIFTV LAILSMILGN VVALAQTSMK
301: RMLAYSSIGQ AGFVMIGFVV GTEAGYASML FYLLVYLFMN LGAFTCVILF SLRTGTDQIS
361: EYAGLYQKDP LLTLGLSLCL LSLGGIPPLA GFFGKIYLFW AGWQAGAYGL VLLGLLTSVI
421: SIYYYIRVVK MMVVKEPQEM SEAVRNYPEV SWSSFGLRPL QVGLVMTVIA TSLAGILANP
481: LFNLVNTAVW DVPQLANQPT VMEVAYQALS PAGKS