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: | Q8DKX9 |
Protein Name: | NADH dehydrogenase subunit 5 |
Length: | 656 |
Molecular Weight: | 71973.00 |
Species: | Thermosynechococcus elongatus (strain BP-1) [197221] |
Number of TMSs: | 17 |
Substrate |
proton |
---|
1: MEPLYQYAWL IPVLPLLGAL IVGFGLIAFS ETTSKLRRPS AIFIMALMAI AMGHSLTLFW
61: SQVQGHLPYT QMIEWAAAGN LHIAMGYVID PLAALMLVIV TTVAFLVMLY SDGYMAHDPG
121: YVRFFAYLSL FGSSMLGLVV SPNLVQVYIF WELVGMCSYL LIGFWYDRKS AAEAAQKAFV
181: TNRVGDFGLL LGMVGLFWAT GTFDFAGMGD RLTELVNTGL LSPSLAAILA ILVFLGPVAK
241: SAQFPLHVWL PDAMEGPTPI SALIHAATMV AAGVFLIARM FPVFEQLPQV MTTIAWTGAF
301: TAFMGATIAI TQNDIKKSLA YSTISQLGYM VMGMGVGAYS AGLFHLMTHA YFKAMLFLGS
361: GSVIHSMEGV VGHNPDLAQD MRYMGGLRKY MPITGATFLV GCLAISGVPP FAGFWSKDEI
421: LGAVFHANPA MWLLTWLTAG LTAFYMFRMY FMTFEGKFRN VPPERQEHHD HHSHHAAVPH
481: ESPWTMTLPL VVLAIPSTLI GFVGTPFNNL FEVFIHAPGE EKVAEHAVDL TEFLILGGSS
541: VGIGLMGITV AYLMYLKGTP SPQAIAKAIQ PLYQFSLHKW YFDELYEAVF IKGCRRLARQ
601: VLEVDYNVVD GVVNLTGFVT MVTGEGLKYL QNGRAQFYAL IVLLAVLGFV IFSVQT