The Enzyme Database

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Accepted name: ferredoxin—quinone oxidoreductase (H+-translocating)
Reaction: 2 reduced ferredoxin [iron-sulfur] cluster + plastoquinone + 6 H+[side 1] = 2 oxidized ferredoxin [iron-sulfur] cluster + plastoquinol + 7 H+[side 2]
Other name(s): NDH-1L complex; NDH-1L′ complex; NDH11 complex; NDH12 complex
Systematic name: ferredoxin:quinone oxidoreductase (H+-translocating)
Comments: The enzyme, present in plants and cyanobacteria, couples electron transport from ferredoxin to plastoquinone and proton pumping from the cytoplasm to the thylakoid lumen. It participates in cyclic electron flow, retuning electrons generated by photosystem I to the plastoquinone pool, thus bypassing the generation of reducing power. It may also participate in respiration using electrons originating from NADPH via the action of EC, ferredoxin—NADP+ reductase (FNR) operating in the direction of ferredoxin reduction. It is a large complex, with some of its subunits resembling those from the bacterial/mitochondrial EC, NADH:ubiquinone reductase (H+-translocating). However, it lacks the NADH-oxidizing module and instead has a module that interacts with ferredoxin. Several forms of the enzyme exist, differing in their exact combination of subunits used. Some of the forms participate in carbon dioxide hydration rather than electron transfer.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Arteni, A.A., Zhang, P., Battchikova, N., Ogawa, T., Aro, E.M. and Boekema, E.J. Structural characterization of NDH-1 complexes of Thermosynechococcus elongatus by single particle electron microscopy. Biochim. Biophys. Acta 1757 (2006) 1469–1475. [DOI] [PMID: 16844076]
2.  Battchikova, N., Wei, L., Du, L., Bersanini, L., Aro, E.M. and Ma, W. Identification of novel Ssl0352 protein (NdhS), essential for efficient operation of cyclic electron transport around photosystem I, in NADPH:plastoquinone oxidoreductase (NDH-1) complexes of Synechocystis sp. PCC 6803. J. Biol. Chem. 286 (2011) 36992–37001. [DOI] [PMID: 21880717]
3.  Yamamoto, H. and Shikanai, T. In planta mutagenesis of Src homology 3 domain-like fold of NdhS, a ferredoxin-binding subunit of the chloroplast NADH dehydrogenase-like complex in Arabidopsis: a conserved Arg-193 plays a critical role in ferredoxin binding. J. Biol. Chem. 288 (2013) 36328–36337. [DOI] [PMID: 24225949]
4.  Ma, W. and Ogawa, T. Oxygenic photosynthesis-specific subunits of cyanobacterial NADPH dehydrogenases. IUBMB Life 67 (2015) 3–8. [DOI] [PMID: 25564967]
5.  Peltier, G., Aro, E.M. and Shikanai, T. NDH-1 and NDH-2 plastoquinone reductases in oxygenic photosynthesis. Annu. Rev. Plant Biol. 67 (2016) 55–80. [DOI] [PMID: 26735062]
6.  Laughlin, T.G., Bayne, A.N., Trempe, J.F., Savage, D.F. and Davies, K.M. Structure of the complex I-like molecule NDH of oxygenic photosynthesis. Nature 566 (2019) 411–414. [DOI] [PMID: 30742075]
7.  Schuller, J.M., Birrell, J.A., Tanaka, H., Konuma, T., Wulfhorst, H., Cox, N., Schuller, S.K., Thiemann, J., Lubitz, W., Setif, P., Ikegami, T., Engel, B.D., Kurisu, G. and Nowaczyk, M.M. Structural adaptations of photosynthetic complex I enable ferredoxin-dependent electron transfer. Science 363 (2019) 257–260. [DOI] [PMID: 30573545]
8.  Zhang, C., Shuai, J., Ran, Z., Zhao, J., Wu, Z., Liao, R., Wu, J., Ma, W. and Lei, M. Structural insights into NDH-1 mediated cyclic electron transfer. Nat. Commun. 11:888 (2020). [DOI] [PMID: 32060291]
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