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Literature summary extracted from
- Oxygenic photosynthesis-specific subunits of cyanobacterial NADPH dehydrogenases (2015), IUBMB Life, 67, 3-8 .
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 7.1.1.10 | thylakoid membrane | - |
Synechocystis sp. PCC 6803 | 42651 | - |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 7.1.1.10 | 2 reduced ferredoxin [iron-sulfur] cluster + plastoquinone + 6 H+[side 1] | Synechocystis sp. PCC 6803 | - |
2 oxidized ferredoxin [iron-sulfur] cluster + plastoquinol + 7 H+[side 2] | - |
? |  |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 7.1.1.10 | Synechocystis sp. PCC 6803 | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 7.1.1.10 | in Synechocystis sp. 6803, some hydrophilic subunits of wild-type NDH-1 complex, including NdhH-NdhK, NdhN, and NdhO, are copurified with photosystem I (PSI), and several PSI subunits, PsaB-PsaD and PsaF, are copurified with NDH-1 by Ni2+ affinity chromatography | Synechocystis sp. PCC 6803 |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 7.1.1.10 | 2 reduced ferredoxin [iron-sulfur] cluster + plastoquinone + 6 H+[side 1] | - |
Synechocystis sp. PCC 6803 | 2 oxidized ferredoxin [iron-sulfur] cluster + plastoquinol + 7 H+[side 2] | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 7.1.1.10 | More | composition, structure, and membrane localization and topology of the different NDH1 complexes, detailed overview | Synechocystis sp. PCC 6803 |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 7.1.1.10 | cyanobacterial NADPH dehydrogenase complex | - |
Synechocystis sp. PCC 6803 |
| 7.1.1.10 | NDH-1 complex | - |
Synechocystis sp. PCC 6803 |
| 7.1.1.10 | NDH-1-like complex | - |
Synechocystis sp. PCC 6803 |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 7.1.1.10 | Ferredoxin | NdhS is suggested to be a ferredoxin (Fd)-binding subunit of chloroplast NDH-1 based on the overall spatial homology of NdhS and the PsaE subunit of PSI complex. Because of a high homology of NdhS in cyanobacterial and chloroplastic NDH-1, cyanobacterial NdhS may also be an Fd-binding subunit. In higher plants, Fd has been suggested to be an exclusive electron donor to chloroplast NDH-1, distinctly different from the electron donor of complex I in nonphotosynthetic organisms. In addition to Fd, NADPH may be another potential electron donor in cyanobacterial NDH-1 | Synechocystis sp. PCC 6803 | |
| 7.1.1.10 | plastoquinone | - |
Synechocystis sp. PCC 6803 | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 7.1.1.10 | evolution | During the evolution from cyanobacteria to higher plants, there are significant changes in the localization and function of certain OPS Ndh subunits despite both cyanobacterial and chloroplastic NDH-1 complexes are classified in a same subclass originating from the complex I family, overview. (i) In cyanobacteria, NdhL-NdhN are localized in the middle of membrane-embedded arm and NdhP is included in the membrane arm. In contrast, in higher plants, NdhL-NdhN are localized in the hydrophilic arm and NdhP (NDF6) is a component of subcomplex B, an exclusive NDH-1 subcomplex in higher plants. (ii) In cyanobacteria, the absence of NdhL does not influence the stability and assembly of NDH-1L and NDH-1M complexes although impaired NDH-CET activity and CO2 uptake. In contrast, knockout of ndhL in higher plants results in entire collapse of hydrophilic arm of chloroplastic NDH-1 complex and consequently complete impairment of NDH-CET. (iii) In cyanobacteria, the deletion of ndhO stabilizes NDH-1 complex and increases NDH-CET activity. In higher plants, knockout of ndhO causes complete impairment of NDH-CET and entire collapse of hydrophilic arm of chloroplastic NDH-1 complex. Such opposite effects may be a result of different roles of cyanobacterial and chloroplastic NdhO in coping with environmental stresses. NdhO in cyanobacteria is suggested to be involved in modulating negatively NDH-CET, whereas NdhO in higher plants may mainly participate in stabilizing chloroplast NDH-1 complex. (iv) NdhQ is present in cyanobacteria but its homologue is absent in higher plants. The severe alteration of these OPS Ndh subunits implies significant changes in the activity of cyanobacterial and chloroplastic NDH-1 enzymes during evolution from cyanobacteria to higher plants. In addition, there are more drastic changes in other Ndh subunits during the evolution. In higher plants, Fd has been suggested to be an exclusive electron donor to chloroplast NDH-1, distinctly different from the electron donor of complex I in nonphotosynthetic organisms. In addition to Fd, NADPH may be another potential electron donor in cyanobacterial NDH-1 (cf. EC 7.1.1.11) | Synechocystis sp. PCC 6803 |
| 7.1.1.10 | malfunction | deletion of NdhQ impairs respiration but not CO2 uptake | Synechocystis sp. PCC 6803 |
| 7.1.1.10 | additional information | identification of seven oxygenic photosynthesis-specific (OPS) subunits of NDH-1 enzyme, NdhL to NdhQ and NdhS. Six of them are also found in higher plants but not in nonphototrophs. NdhQ appears to be present only in NDH-1L complex. In addition to these subunits, the NDH-1L complex contains NdhD1, NdhF1, NdhP, and NdhQ, and the NDH-1L' complex, which remains elusive, may include NdhD2 and NdhF1. Complex NDH-1S is composed of NdhD3, NdhF3, CupA, and CupS, whereas complex NDH-1S' is made up of NdhD4, NdhF4, and CupB. In Synechocystis sp. 6803, some hydrophilic subunits of wild-type NDH-1 complex, including NdhH-NdhK, NdhN, and NdhO, are copurified with photosystem I (PSI), and several PSI subunits, PsaB-PsaD and PsaF, are copurified with NDH-1 | Synechocystis sp. PCC 6803 |
| 7.1.1.10 | physiological function | the enzyme commplex participates in a variety of bioenergetic reactions, including respiration, cyclic electron transport around photosystem I and CO2 uptake. Certain role of cyanobacterial and chloroplastic NDH-1 in photosynthetic reactions for the identified sseven OPS subunits of cyanobacterial NDH-1, overview. NdhS might have a common role in binding the reduced Fd from PSI in the catalytic domain of NDH-1 enzymes | Synechocystis sp. PCC 6803 |
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