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Literature summary for 7.1.1.10 extracted from

  • Zhang, C.; Shuai, J.; Ran, Z.; Zhao, J.; Wu, Z.; Liao, R.; Wu, J.; Ma, W.; Lei, M.
    Structural insights into NDH-1 mediated cyclic electron transfer (2020), Nat. Commun., 11, 888 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 7.1.1.10

Localization

Localization Comment Organism GeneOntology No. Textmining
thylakoid membrane
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 Thermosynechococcus vestitus 42651
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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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 ?
2 reduced ferredoxin [iron-sulfur] cluster + plastoquinone + 6 H+[side 1] Thermosynechococcus vestitus NIES-2133
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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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Thermosynechococcus vestitus NIES-2133 Q8DKZ3
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 reduced ferredoxin [iron-sulfur] cluster + plastoquinone + 6 H+[side 1]
-
 Thermosynechococcus vestitus 2 oxidized ferredoxin [iron-sulfur] cluster + plastoquinol + 7 H+[side 2]
-
 ?
2 reduced ferredoxin [iron-sulfur] cluster + plastoquinone + 6 H+[side 1]
-
 Thermosynechococcus vestitus NIES-2133 2 oxidized ferredoxin [iron-sulfur] cluster + plastoquinol + 7 H+[side 2]
-
 ?

Subunits

Subunits Comment Organism
More analysis of the 3.2-A-resolution cryo-EM structure of the ferredoxin (Fd)-NDH-1L complex from Thermosynechococcus elongatus, NdhS is a constitutive component of NDH-1L and adopts an SH3-like fold, it is the Fd-binding subunit in NDH-1L. But it is unlikely NdhS plays a major role in direct Fd binding, even though the C-terminal 10-residue tail of NdhS is not visible in the EM density. It is more likely that NdhS makes its contribution indirectly as a foothold holding the transient NdhV in the NDH-1L complex for Fd binding. NdhS is required for accumulation of NdhV in the thylakoid membranes but not vice versa. NdhV is a transient subunit of NDH-1L, NdhV can function as an Fd-binding cofactor, guiding the association of Fd to the NDH-1L complex. NdhV may also accelerate the electron transfer rate by helping stabilize the Fd-NdhI interface in an electron transfer-competent conformation. NdhO might be a negative regulator of NDH-CET activity. The Fd-NDH-1L complex structure reveals that all four OPS regulatory subunits are in close vicinity to the electron transport pathway in NDH-1L-NdhL adjacent to the electron acceptor PQ cavity while NdhV, NdhS, and NdhO are at the electron donor Fd-binding site. The peripheral arm of NDH-1L adopts a cylinder-shaped architecture organized by four conserved core subunits (NdhH-NdhK) and two OPS structural subunits (NdhM and NdhN). The central axis of the cylinder is the redox chain of three [4Fe-4S] clusters composed of distal and medial clusters N6a and N6b coordinated in NdhI and terminal cluster. OPS regulatory subunits NdhS, NdhV, and NdhO all fold into small compact structures, binding to the apex of the peripheral arm. NdhS stably sits in a groove of NdhI, holding NdhV to attach to and buttress NdhI for Fd binding and electron transfer. On the opposite side of NdhI, NdhO is secured on the surface of the peripheral arm through interactions with NdhJ, NdhK, and NdhN Thermosynechococcus vestitus

Synonyms

Synonyms Comment Organism
NDH-1
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 Thermosynechococcus vestitus

Cofactor

Cofactor Comment Organism Structure
additional information hydrophobic cofactors identified in the Fd-NDH-1L complex structure, i.e. beta-carotene, dipalmitoylphosphatidylglycerol, sulfoquinovosyldiacylglycerol, and digalactosyldiacylglycerol, overview Thermosynechococcus vestitus

General Information

General Information Comment Organism
evolution photosynthetic NDH-1L and respiratory complex I share a conserved L-shaped skeleton and are suggested to originate commonly from a group 4 membrane-bound [NiFe] hydrogenase that accepts electron from ferredoxin (Fd). During evolution, however, respiratory complex I and photosynthetic NDH-1L developed different catalytic reactions. An NADH-binding module consisting of three subunits is capable of oxidizing NADH in the respiratory complex I. But the counterpart of this NADH-binding-module is absent in the photosynthetic NDH-1L complex. The photosynthetic NDH-1L complex retains an original electron input module that accepts electrons from Fd Thermosynechococcus vestitus
malfunction deletion of NdhS causes a similar level of defect in the NDHCET activity as in DELTAndhV cells in response to high-light irradiation Thermosynechococcus vestitus
metabolism NDH-1 is a key component of the cyclic-electron-transfer around photosystem I (PSI CET) pathway, an important antioxidant mechanism for efficient photosynthesis Thermosynechococcus vestitus
physiological function the NDH-1MS complex without NdhO is induced to accelerate the NDH-CET activity by long-term high-light irradiation. Enzyme domains and 10 complex components (NdhJ, NdhO, NdhV, NdhI, NdhS, NdhH, NdhM, NdhN, NdhK, and Fd), structure-function relationship, overview Thermosynechococcus vestitus