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: | Q8DL31 |
Protein Name: | NAD(P)H-quinone oxidoreductase subunit I |
Length: | 196 |
Molecular Weight: | 22416.00 |
Species: | Thermosynechococcus elongatus (strain BP-1) [197221] |
Location1 / Topology2 / Orientation3: |
Cellular thylakoid membrane1 / Peripheral membrane protein2 |
Substrate |
proton |
---|
1: MKFLNQITNY AKEAVQSAKY IGQGLSVTFD HMRRRPITVQ YPYEKLIPSE RFRGRIHFEF
61: DKCIACEVCV RVCPINLPVV DWVFNKELKK KELKHYSIDF GVCIFCANCV EYCPTNCLSV
121: TEEYELATYD RHELNYDSVA MGRIPYKVTQ DPMVTPIREF AYLPAGVMSG HDLPAGAQRA
181: GERPEAIANT AKSSEN