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Literature summary for 7.1.1.10 extracted from

  • Laughlin, T.; Bayne, A.; Trempe, J.; Savage, D.; Davies, K.
    Structure of the complex I-like molecule NDH ofxa0oxygenic photosynthesis (2019), Nature, 566, 411-414 .
    View publication on PubMed
Search for more literature for 7.1.1.10

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 reduced ferredoxin [iron-sulfur] cluster + plastoquinone + 6 H+[side 1] Thermosynechococcus vestitus
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 2 oxidized ferredoxin [iron-sulfur] cluster + plastoquinol + 7 H+[side 2]
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 ?

Organism

Organism UniProt Comment Textmining
Thermosynechococcus vestitus Q8DKZ3
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Reaction

Reaction Comment Organism Reaction ID
2 reduced ferredoxin [iron-sulfur] cluster + plastoquinone + 6 H+[side 1] = 2 oxidized ferredoxin [iron-sulfur] cluster + plastoquinol + 7 H+[side 2] proposed models for the electron-transfer mechanism of NDH, overview. NDH could possess several electron transfer routes, which would serve to maximize plastoquinone reduction and avoid deleterious off-target chemistry of the semi-plastoquinone radical Thermosynechococcus vestitus
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 reduced ferredoxin [iron-sulfur] cluster + plastoquinone + 6 H+[side 1]
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 Thermosynechococcus vestitus 2 oxidized ferredoxin [iron-sulfur] cluster + plastoquinol + 7 H+[side 2]
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 ?
2 reduced ferredoxin [iron-sulfur] cluster + plastoquinone + 6 H+[side 1] the OPS subunits, specifically NdhS, enable NDH to accept electrons from its electron donor, ferredoxin Thermosynechococcus vestitus 2 oxidized ferredoxin [iron-sulfur] cluster + plastoquinol + 7 H+[side 2]
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 ?

Subunits

Subunits Comment Organism
More NDH adopts an L-shaped structure that is characteristic of respiratory NADH dehydrogenase complexes. NDH possesses 11 of the 14 core complex I subunits, as well as several oxygenic-photosynthesis-specific (OPS) subunits that are conserved from cyanobacteria to plants. However, the three core complex I subunits that are involved in accepting electrons from NAD(P)H are notably absent in NDH. OPS subunits NdhO and NdhS and the beta-hairpin of core subunit NdhI, surface model, structure-function analysis, overview Thermosynechococcus vestitus

Synonyms

Synonyms Comment Organism
complex I-like molecule NDH
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 Thermosynechococcus vestitus

Cofactor

Cofactor Comment Organism Structure
Ferredoxin the OPS subunits, specifically NdhS, enable NDH to accept electrons from its electron donor, ferredoxin Thermosynechococcus vestitus
plastoquinone
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 Thermosynechococcus vestitus
[4Fe-4S] cluster
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 Thermosynechococcus vestitus

General Information

General Information Comment Organism
evolution NDH possesses 11 of the 14 core complex I subunits, as well as several oxygenic-photosynthesis-specific (OPS) subunits that are conserved from cyanobacteria to plants. However, the three core complex I subunits that are involved in accepting electrons from NAD(P)H are notably absent in NDH. NDH adopts an L-shaped structure that is characteristic of respiratory NADH dehydrogenase complexes Thermosynechococcus vestitus
additional information the OPS subunits, specifically NdhS, enable NDH to accept electrons from its electron donor, ferredoxin. Analysis of the arrangement of redox chain and cofactors within the peripheral arm, structure-function analysis, overview Thermosynechococcus vestitus
physiological function cyclic electron flow around photosystem I (PSI) is a mechanism by which photosynthetic organisms balance the levels of ATP and NADPH necessary for efficient photosynthesis. NAD(P)H dehydrogenase-like complex (NDH) is a key component of this pathway in most oxygenic photosynthetic organisms and is the last large photosynthetic membrane-protein complex. NDH transfers electrons originating from PSI to the plastoquinone pool while pumping protons across the thylakoid membrane, thereby increasing the amount of ATP produced per NADP+ molecule reduced. Mechanism of NDH acquiring and transfering electrons to plastoquinone, overview. The location of the OPS subunits supports a role in electron transfer and defines two potential ferredoxin-binding sites at the apex of the peripheral arm. NDH could possess several electron transfer routes, which would serve to maximize plastoquinone reduction and avoid deleterious off-target chemistry of the semi-plastoquinone radical Thermosynechococcus vestitus