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Literature summary for 7.1.1.10 extracted from

  • Saura, P.; Kaila, V.R.I.
    Molecular dynamics and structural models of the cyanobacterial NDH-1 complex (2019), Biochim. Biophys. Acta, 1860, 201-208 .
    View publication on PubMedView publication on EuropePMC

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast
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Synechocystis sp. PCC 6803 9507
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membrane the proton pumping subunits of NDH-1 are located in the membrane domain of the enzyme, and comprise subunits NdhA, NdhC, NdhE, NdhG, in addition to NdhB, NdhD1 (D2), and NdhF1 in the NDH-1L (NDH-1L') isoform Synechocystis sp. PCC 6803 16020
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Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ FeS centers, N6a, N6b, and N2, showing edge-to-edge distances between the clusters Synechocystis sp. PCC 6803

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] Synechocystis sp. PCC 6803
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2 oxidized ferredoxin [iron-sulfur] cluster + plastoquinol + 7 H+[side 2]
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?

Organism

Organism UniProt Comment Textmining
Synechocystis sp. PCC 6803
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-
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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]
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Synechocystis sp. PCC 6803 2 oxidized ferredoxin [iron-sulfur] cluster + plastoquinol + 7 H+[side 2]
-
?
2 reduced ferredoxin [iron-sulfur] cluster + plastoquinone + 6 H+[side 1] NDH-I operates with ferredoxin, that binds to NDH-S subunit. Electrons are transferred from ferredoxin (Fd) to plastoquinone (PQ) in the ca. 60 A long hydrophilic domain, and the released free energy is employed for proton pumping across the ca. 200 A membrane domain. The electron transfer process in NDH-1 is likely to be kinetically limited by the diffusion of ferredoxin. The redox potential of cyanobacterial ferredoxin is in the ca. -420 mV range [49], i.e., 100 mV lower than the electron donor NADH in complex I. This small redox drop from ferredoxin to N2 may thus help to drive the electrons to PQ, to stepwise reduce PQ via PQ-/radical to plastoquinol (PQH2) Synechocystis sp. PCC 6803 2 oxidized ferredoxin [iron-sulfur] cluster + plastoquinol + 7 H+[side 2]
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?

Subunits

Subunits Comment Organism
More the the NDH-1 complex is composed of subunits NdhA, NdhB, NdhC, NdhD1, NdhD3, NdhE, NdhF1, NdhF3, NdhG, NdhH, NdhI, NdhJ, and NdhK, plus the ferredoxin binding component NdhS Synechocystis sp. PCC 6803

Synonyms

Synonyms Comment Organism
cyanobacterial NDH-1 complex
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Synechocystis sp. PCC 6803
cyanobacterial type-I NADH dehydrogenase complex
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Synechocystis sp. PCC 6803
NDH-1
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Synechocystis sp. PCC 6803
NDH-1L
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Synechocystis sp. PCC 6803
NDH-1MS
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Synechocystis sp. PCC 6803

Cofactor

Cofactor Comment Organism Structure
Fe-S center FeS centers, N6a, N6b, and N2, showing edge-to-edge distances between the clusters Synechocystis sp. PCC 6803
Ferredoxin in contrast to the respiratory complex I, which receives electrons from NADH via FMN across a ca. 100 A-long chain of 8-9 FeS centers, ferredoxin has been suggested to bind to subunit NdhS, and provide electrons directly to the N6a center Synechocystis sp. PCC 6803
plastoquinone in contrast to complex I, which employs ubiquinone or menaquinone, the NDH-1 complex operates with plastoquinone. The PQ binding site and its edge-to-edge distance to N2. The figure also shows an electrostatic wire connecting the PQ site to the NdhA subunit (in green) of the membrane domain Synechocystis sp. PCC 6803

General Information

General Information Comment Organism
evolution NDH-1 is structurally related to respiratory complex I (NADH:ubiquinone oxidoreductase), but unlike the latter, the cyanobacterial enzyme supports cyclic electron flow around photosystem I as well as inorganic carbon uptake via CO2. NDH-1 is also present in plants and algae that harbor the respiratory and photosynthetic machineries in their mitochondria and chloroplasts, respectively. NdhS is homologous to the Src homology 3 domain-like fold found in the ferredoxin-binding site of PSI, and it may thus mediate binding of the electron donor ferredoxin to NDH-1 Synechocystis sp. PCC 6803
additional information NDH-1 is expressed in different isoforms. The NDH-1L and NDH-1L' isoforms support respiration and cyclic electron flow, whereas NDH-1MS and NDH-1MS' are involved in CO2 uptake. Moreover, the NDH-1L' and NDH-1MS' isoforms are constitutive, whereas the NDH-1L and NDH-1MS isoforms are expressed under low CO2 concentrations. All NDH-1 isoforms contain a hydrophilic domain with subunits NdhI/J/K/H harboring three ironsulfur (FeS) centers, N6a, N6b, and N2. In contrast to the respiratory complex I, which receives electrons from NADH via FMN across a ca. 100 A-long chain of 8-9 FeS centers, ferredoxin has been suggested to bind to subunit NdhS, and provide electrons directly to the N6a center. NdhS is homologous to the Src homology 3 domain-like fold found in the ferredoxin-binding site of PSI, and it may thus mediate binding of the electron donor ferredoxin to NDH-1. NDH-1 complex and proton channels structure-function analysis, molecular models of the cyanobacterial NDH-1 showing the NDH-1L isoform and NDH-1MS isoform, homology structure modeling, molecular dynamics simulations, detailed overview Synechocystis sp. PCC 6803
physiological function the two NDH-1 isoforms are involved in redox-driven proton pumping (NDH-1L) and CO2-fixation (NDH-1MS) Synechocystis sp. PCC 6803