Literature summary extracted from

Gao, F.; Zhao, J.; Chen, L.; Battchikova, N.; Ran, Z.; Aro, E.; Ogawa, T.; Ma, W.
The NDH-1L-PSI supercomplex is important for efficient cyclic electron transport in cyanobacteria (2016), Plant Physiol., 172, 1451-1464 .

Cloned(Commentary)

EC Number	Cloned (Comment)	Organism
7.1.1.10	construction of a wild-type-CpcG2-YFP-His6 strain by adding the YFP-His6 tag on the C-terminus of CpcG2 in the wild-type background. PCR analysis indicates complete segregation of the tagged gene. Recombinant complex expression in Synechocystis sp. 6803. Complex analysis by liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis, immunoblot and coimmunoprecipitation	Synechocystis sp. PCC 6803

Protein Variants

EC Number	Protein Variants	Comment	Organism
7.1.1.10	additional information	reoxidation of P700 is much faster in DELTAcpcG2 than in the wild-type. Furthermore, the rereduction rate of P700+ was monitored in darkness after the illumination of 3-(3,4-dichlorophenyl)-1,1-dimethylurea (DCMU)-treated cells with FR. The rereduction of P700+ is much slower in DELTAcpcG2 than in the wild-type, providing evidence of the scarcity of CET from reduced Fd via NDH-1 back to P700+ in darkness. Therefore, the slow growth of DELTAcpcG2 under high-light conditions can be attributed to the low NDH-CET activity. Complex analysis by liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis, immunoblot and coimmunoprecipitation	Synechocystis sp. PCC 6803

General Stability

EC Number	General Stability	Organism
7.1.1.10	the photosystem I-associated linker protein CpcL, i.e. CpcG2, is essential to stabilize NDH-1L and NDH-1M complexes	Synechocystis sp. PCC 6803

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	recombinant wild-type and mutant CpcG2-YFP-His6 supercomplex from Synechocystis sp. 6803 thylakoid membranes by Ni2+ affinity chromatography	Synechocystis sp. PCC 6803

Source Tissue

EC Number	Source Tissue	Comment	Organism	Textmining

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	determination of the presence of a supercomplex composed of NDH-1, CpcG2, and PSI (NDH-1-CpcG2-PBS-PSI), structure-function relationship and analysis, overview	Synechocystis sp. PCC 6803

Synonyms

EC Number	Synonyms	Comment	Organism
7.1.1.10	NDH-1L	-	Synechocystis sp. PCC 6803

Cofactor

EC Number	Cofactor	Comment	Organism	Structure
7.1.1.10	Ferredoxin	-	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	NDH-1 complexes belong to the complex I family. On the basis of sequence similarity analysis, the complex I family is suggested to originate from a common ancestor, a group 4 membrane-bound [NiFe] hydrogenase that possesses a proton-transporting hydrogen:ferredoxin (Fd) oxidoreductase activity. During evolution, respiratory NDH-1 and photosynthetic NDH-1 developed different catalytic activities. The former has become equipped with a new NADH-oxidizing module consisting of three subunits and capable of oxidizing NADH, And the latter has retained an original electron input module that accepts electrons from Fd. Structurally, respiratory NDH-1 and photosynthetic NDH-1 contain a conserved L-shaped skeleton	Synechocystis sp. PCC 6803
7.1.1.10	malfunction	isolation of NDH-CET-defective mutants. Under high-light conditions, the growth of NDH-CET-defective mutants, such as DELTAndhS, is markedly slower in comparison with the wild-type despite similar growth undermoderate light irradiation. Inactivation of cpcG2 impairs NDH-CET activity. Deletion of CpcG2 destabilizes NDH-1L as well as its degradation product NDH-1M and significantly decreases the number of functional photosystem I (PSI) centers, consistent with the involvement of CpcG2 in NDH-1-dependent cyclic electron transport. The CpcG2 deletion, however, has no effect on respiration. The NDH-1L-CpcG2-PSI supercomplex is absent in the cpcG2 deletion mutant, the PSIless mutant, and several other strains deficient in NDH-1L and/or NDH-1M	Synechocystis sp. PCC 6803
7.1.1.10	additional information	determination of the presence of a supercomplex composed of NDH-1, CpcG2, and PSI (NDH-1-CpcG2-PBS-PSI), structure-function relationship and analysis, overview	Synechocystis sp. PCC 6803
7.1.1.10	physiological function	the photosystem I-associated linker protein CpcL, i.e. CpcG2, is essential to stabilize NDH-1L and NDH-1M complexes, interaction analysis of CpcG2 with NDH-1 and PSI complexes. The formation of an NDH-1L-CpcG2-PSI supercomplex in cyanobacteria facilitates photosystem I (PSI) cyclic electron transport via NDH-1L. Cyclic electron transport (CET) around PSI is an important process for oxygenic photosynthetic organisms. In cooperation with linear electron transport, CET contributes to the formation of a proton gradient across the thylakoid membrane, which increases the production of ATP in relation to NADPH and consequently optimizes the ATP/NADPHratio. In addition, CET plays an important role in protecting photosynthesis against various environmental stresses, such as high light. In cyanobacteria, the main route for CET involves NDH-1 complexes, which belong to the complex I family	Synechocystis sp. PCC 6803

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Release 2023.1 (January 2023)