Literature summary for 7.1.1.10 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 .

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Cloned(Commentary)

Cloned (Comment)	Organism
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

Protein Variants	Comment	Organism
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

General Stability	Organism
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

Localization	Comment	Organism	GeneOntology No.	Textmining
thylakoid membrane	-	Synechocystis sp. PCC 6803	42651	-

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	-	2 oxidized ferredoxin [iron-sulfur] cluster + plastoquinol + 7 H+[side 2]	-	?

Organism

Organism	UniProt	Comment	Textmining
Synechocystis sp. PCC 6803	-	-	-

Purification (Commentary)

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

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
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

Subunits	Comment	Organism
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

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

Cofactor

Cofactor	Comment	Organism	Structure
Ferredoxin	-	Synechocystis sp. PCC 6803
plastoquinone	-	Synechocystis sp. PCC 6803

General Information

General Information	Comment	Organism
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
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
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
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)