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Literature summary for 7.1.1.10 extracted from
- NDH-1 and NDH-2 plastoquinone reductases in oxygenic photosynthesis (2016), Annu. Plant Biol., 67, 55-80 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| the Synechocystis sp. PCC6803 genome contains six different ndhD genes (ndhD1-6) and three different ndhF genes (ndhF1, ndhF3, and ndhF4) | Synechocystis sp. PCC 6803 |
| the Synechocystis sp. PCC6803 genome contains six different ndhD genes (ndhD1-6) and three different ndhF genes (ndhF1, ndhF3, and ndhF4) | Thermosynechococcus vestitus |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| chloroplast | - |
Nicotiana tabacum | 9507 | - |
| chloroplast | - |
Arabidopsis thaliana | 9507 | - |
| chloroplast | - |
Physcomitrium patens | 9507 | - |
| chloroplast | - |
Marchantia polymorpha | 9507 | - |
| thylakoid membrane | - |
Synechocystis sp. PCC 6803 | 42651 | - |
| thylakoid membrane | - |
Thermosynechococcus vestitus | 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] | Nicotiana tabacum | - |
2 oxidized ferredoxin [iron-sulfur] cluster + plastoquinol + 7 H+[side 2] | - |
? |  |
| 2 reduced ferredoxin [iron-sulfur] cluster + plastoquinone + 6 H+[side 1] | Arabidopsis thaliana | - |
2 oxidized ferredoxin [iron-sulfur] cluster + plastoquinol + 7 H+[side 2] | - |
? | |
| 2 reduced ferredoxin [iron-sulfur] cluster + plastoquinone + 6 H+[side 1] | Physcomitrium patens | - |
2 oxidized ferredoxin [iron-sulfur] cluster + plastoquinol + 7 H+[side 2] | - |
? | |
| 2 reduced ferredoxin [iron-sulfur] cluster + plastoquinone + 6 H+[side 1] | Marchantia polymorpha | - |
2 oxidized ferredoxin [iron-sulfur] cluster + plastoquinol + 7 H+[side 2] | - |
? | |
| 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] | - |
? | |
| 2 reduced ferredoxin [iron-sulfur] cluster + plastoquinone + 6 H+[side 1] | Thermosynechococcus vestitus | - |
2 oxidized ferredoxin [iron-sulfur] cluster + plastoquinol + 7 H+[side 2] | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Arabidopsis thaliana | - |
- |
- |
| Marchantia polymorpha | - |
- |
- |
| Nicotiana tabacum | - |
- |
- |
| no activity in Chlamydomonas reinhardtii | - |
- |
- |
| Physcomitrium patens | - |
- |
- |
| Synechocystis sp. PCC 6803 | - |
- |
- |
| Thermosynechococcus vestitus | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2 reduced ferredoxin [iron-sulfur] cluster + plastoquinone + 6 H+[side 1] | - |
Nicotiana tabacum | 2 oxidized ferredoxin [iron-sulfur] cluster + plastoquinol + 7 H+[side 2] | - |
? | |
| 2 reduced ferredoxin [iron-sulfur] cluster + plastoquinone + 6 H+[side 1] | - |
Arabidopsis thaliana | 2 oxidized ferredoxin [iron-sulfur] cluster + plastoquinol + 7 H+[side 2] | - |
? | |
| 2 reduced ferredoxin [iron-sulfur] cluster + plastoquinone + 6 H+[side 1] | - |
Physcomitrium patens | 2 oxidized ferredoxin [iron-sulfur] cluster + plastoquinol + 7 H+[side 2] | - |
? | |
| 2 reduced ferredoxin [iron-sulfur] cluster + plastoquinone + 6 H+[side 1] | - |
Marchantia polymorpha | 2 oxidized ferredoxin [iron-sulfur] cluster + plastoquinol + 7 H+[side 2] | - |
? | |
| 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] | - |
? | |
| 2 reduced ferredoxin [iron-sulfur] cluster + plastoquinone + 6 H+[side 1] | - |
Thermosynechococcus vestitus | 2 oxidized ferredoxin [iron-sulfur] cluster + plastoquinol + 7 H+[side 2] | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | different NDH-1 complexes are found in the cyanobacterial thylakoid membrane. All of these complexes contain the NDH-1M module, which is composed of both hydrophilic and hydrophobic domains and is presently known to comprise 14 subunits (NdhA-C, NdhE, NdhG-O, and NdhS). NDH-1M has no physiological function by itself but represents an assembly intermediate for functional NDH-1 complexes. The NdhH-K, NdhO, and NdhS subunits form the hydrophilic domain, while the NdhA-C, NdhE, NdhG, and NdhL-N subunits are components of the hydrophobic membrane domain. The NdhO subunit, assigned to the hydrophobic domain, is shown to strongly interact with the NdhI and NdhK subunits of the hydrophilic domain, thereby providing flexibility and maximal NDH-dependent cyclic electron transport (NDH-CET) activity under high-light conditions. The NdhS subunit of the hydrophilic domain of NDH-1M is essential for binding of Fd, the putative electron donor to cyanobacterial NDH-1 complexes, as in the case of plant chloroplasts | Thermosynechococcus vestitus |
| More | different NDH-1 complexes are found in the cyanobacterial thylakoid membrane. All of these complexes contain the NDH-1M module, which is composed of both hydrophilic and hydrophobic domains and is presently known to comprise 14 subunits (NdhA-C, NdhE, NdhG-O, and NdhS). NDH-1M has no physiological function by itself but represents an assembly intermediate for functional NDH-1 complexes. The NdhH-K, NdhO, and NdhS subunits form the hydrophilic domain, while the NdhA-C, NdhE, NdhG, and NdhL-N subunits are components of the hydrophobic membrane domain. The NdhO subunit, assigned to the hydrophobic domain, is shown to strongly interact with the NdhI and NdhK subunits of the hydrophilic domain, thereby providing flexibility and maximal NDH-dependent cyclic electron transport (NDH-CET) activity under high-light conditions. The NdhS subunit of the hydrophilic domain of NDH-1M is essential for binding of Fd, the putative electron donor to cyanobacterial NDH-1 complexes, as in the case of plant chloroplasts. The maturation factor, the Slr1097 (CRR6) protein, is involved in complex assembly in Synechocystis sp. PCC6803. The Synechocystis sp. PCC6803 genome contains six different ndhD genes (ndhD1-6) and three different ndhF genes (ndhF1, ndhF3, and ndhF4) | Synechocystis sp. PCC 6803 |
| More | the subunit composition of the plant NDH-1 complex, overview. Chloroplast NDH-1 is structurally subdivided into five subcomplexes: A, B, M (membrane), L (lumen), and ED (electron donor). The 11 plastid-encoded subunits (NdhA-K) are conserved in all NDH-related protein complexes and form an L-shaped skeleton. Chloroplast NDH-1 is a large protein complex consisting of these 11 subunits and more than 19 nucleus-encoded subunits. Subcomplex A corresponds to the Q module of respiratory NADH dehydrogenases and includes four plastid-encoded subunits (NdhH-K). All the cofactors required for electron transport, from the soluble electron donor to the complex to plastoquinone (PQ), are probably harbored by these subunits. Chloroplast NDH-1 includes four additional nuclear-encoded subunits (NdhL-O). Subcomplex M consists of seven plastid-encoded subunits (NdhA-G) and forms the membrane arm that functions in proton translocation across the membrane (the P module in respiratory NADH dehydrogenase). Subcomplex B is composed of five subunits (PnsB1-5) and is specific to chloroplast NDH-1. PnsB4 and PnsB5 have transmembrane domains, whereas PnsB1, PnsB2, and PnsB3 are localized to the stroma side, probably anchored on PnsB4 and PnsB5. Although the molecular function of subcomplex B remains unelucidated, defects in its subunits result in the destabilization of the total complex. Subcomplex L contains at least five subunits (PnsL1-5) and is also specific to chloroplast NDH-1. Phylogenetically, the occurrence of subcomplex L is linked to the formation of a supercomplex between NDH-1 and PSI. Three of the subcomplex L subunits (PnsL1-3) show sequence similarities to lumenal subunits of PSII: PnsL1 is PsbP-like protein 2 (PPL2), and PnsL2 and PnsL3 are forms of PsbQ-like protein (PQL). In PSII, PsbP and PsbQ stabilize the PSII supercomplex by interacting with CP26 and CP47, supporting the idea that subcomplex L stabilizes the NDH-1-PSI supercomplex at the lumen side. Three subunits of subcomplex ED - NdhS, NdhT, and NdhU - have been identified by proteomic analysis of the NDH-1-PSI supercomplex. NdhS is involved in ferredoxin (Fd) binding. NdhT and NdhU are J and J-like proteins, respectively, that have a transmembrane domain and likely form a heterodimer required for stabilizing NdhS. NdhV is a subunit loosely bound to subcomplex ED, forming the most fragile part of the complex. Subcomplex ED interacts with subcomplex A to form the Fd-binding site, which includes the Fd-oxidizing site | Nicotiana tabacum |
| More | the subunit composition of the plant NDH-1 complex, overview. Chloroplast NDH-1 is structurally subdivided into five subcomplexes: A, B, M (membrane), L (lumen), and ED (electron donor). The 11 plastid-encoded subunits (NdhA-K) are conserved in all NDH-related protein complexes and form an L-shaped skeleton. Chloroplast NDH-1 is a large protein complex consisting of these 11 subunits and more than 19 nucleus-encoded subunits. Subcomplex A corresponds to the Q module of respiratory NADH dehydrogenases and includes four plastid-encoded subunits (NdhH-K). All the cofactors required for electron transport, from the soluble electron donor to the complex to plastoquinone (PQ), are probably harbored by these subunits. Chloroplast NDH-1 includes four additional nuclear-encoded subunits (NdhL-O). Subcomplex M consists of seven plastid-encoded subunits (NdhA-G) and forms the membrane arm that functions in proton translocation across the membrane (the P module in respiratory NADH dehydrogenase). Subcomplex B is composed of five subunits (PnsB1-5) and is specific to chloroplast NDH-1. PnsB4 and PnsB5 have transmembrane domains, whereas PnsB1, PnsB2, and PnsB3 are localized to the stroma side, probably anchored on PnsB4 and PnsB5. Although the molecular function of subcomplex B remains unelucidated, defects in its subunits result in the destabilization of the total complex. Subcomplex L contains at least five subunits (PnsL1-5) and is also specific to chloroplast NDH-1. Phylogenetically, the occurrence of subcomplex L is linked to the formation of a supercomplex between NDH-1 and PSI. Three of the subcomplex L subunits (PnsL1-3) show sequence similarities to lumenal subunits of PSII: PnsL1 is PsbP-like protein 2 (PPL2), and PnsL2 and PnsL3 are forms of PsbQ-like protein (PQL). In PSII, PsbP and PsbQ stabilize the PSII supercomplex by interacting with CP26 and CP47, supporting the idea that subcomplex L stabilizes the NDH-1-PSI supercomplex at the lumen side. Three subunits of subcomplex ED - NdhS, NdhT, and NdhU - have been identified by proteomic analysis of the NDH-1-PSI supercomplex. NdhS is involved in ferredoxin (Fd) binding. NdhT and NdhU are J and J-like proteins, respectively, that have a transmembrane domain and likely form a heterodimer required for stabilizing NdhS. NdhV is a subunit loosely bound to subcomplex ED, forming the most fragile part of the complex. Subcomplex ED interacts with subcomplex A to form the Fd-binding site, which includes the Fd-oxidizing site | Physcomitrium patens |
| More | the subunit composition of the plant NDH-1 complex, overview. Chloroplast NDH-1 is structurally subdivided into five subcomplexes: A, B, M (membrane), L (lumen), and ED (electron donor). The 11 plastid-encoded subunits (NdhA-K) are conserved in all NDH-related protein complexes and form an L-shaped skeleton. Chloroplast NDH-1 is a large protein complex consisting of these 11 subunits and more than 19 nucleus-encoded subunits. Subcomplex A corresponds to the Q module of respiratory NADH dehydrogenases and includes four plastid-encoded subunits (NdhH-K). All the cofactors required for electron transport, from the soluble electron donor to the complex to plastoquinone (PQ), are probably harbored by these subunits. Chloroplast NDH-1 includes four additional nuclear-encoded subunits (NdhL-O). Subcomplex M consists of seven plastid-encoded subunits (NdhA-G) and forms the membrane arm that functions in proton translocation across the membrane (the P module in respiratory NADH dehydrogenase). Subcomplex B is composed of five subunits (PnsB1-5) and is specific to chloroplast NDH-1. PnsB4 and PnsB5 have transmembrane domains, whereas PnsB1, PnsB2, and PnsB3 are localized to the stroma side, probably anchored on PnsB4 and PnsB5. Although the molecular function of subcomplex B remains unelucidated, defects in its subunits result in the destabilization of the total complex. Subcomplex L contains at least five subunits (PnsL1-5) and is also specificto chloroplast NDH-1. Phylogenetically, the occurrence of subcomplex L is linked to the formation of a supercomplex between NDH-1 and PSI. Three of the subcomplex L subunits (PnsL1-3) show sequence similarities to lumenal subunits of PSII: PnsL1 is PsbP-like protein 2 (PPL2), and PnsL2 and PnsL3 are forms of PsbQ-like protein (PQL). In PSII, PsbP and PsbQ stabilize the PSII supercomplex by interacting with CP26 and CP47, supporting the idea that subcomplex L stabilizes the NDH-1-PSI supercomplex at the lumen side. Three subunits of subcomplex ED - NdhS, NdhT, and NdhU - have been identified by proteomic analysis of the NDH-1-PSI supercomplex. NdhS is involved in ferredoxin (Fd) binding. NdhT and NdhU are J and J-like proteins, respectively, that have a transmembrane domain and likely form a heterodimer required for stabilizing NdhS. NdhV is a subunit loosely bound to subcomplex ED, forming the most fragile part of the complex. Subcomplex ED interacts with subcomplex A to form the Fd-binding site, which includes the Fd-oxidizing site | Marchantia polymorpha |
| More | the subunit composition of the plant NDH-1 complex, overview. Chloroplast NDH-1 is structurally subdivided into five subcomplexes: A, B, M (membrane), L (lumen), and ED (electron donor). The 11 plastid-encoded subunits (NdhA-K) are conserved in all NDH-related protein complexes and form an L-shaped skeleton. Chloroplast NDH-1 is a large protein complex consisting of these 11 subunits and more than 19 nucleus-encoded subunits. Subcomplex A corresponds to the Q module of respiratory NADH dehydrogenases and includes four plastid-encoded subunits (NdhH-K). All the cofactors required for electron transport, from the soluble electron donor to the complex to plastoquinone (PQ), are probably harbored by these subunits.ChloroplastNDH-1includes four additional nuclear-encoded subunits (NdhL-O). Subcomplex M consists of seven plastid-encoded subunits (NdhA-G) and forms the membrane arm that functions in proton translocation across the membrane (the P module in respiratory NADH dehydrogenase). Subcomplex B is composed of five subunits (PnsB1-5) and is specific to chloroplast NDH-1. PnsB4 and PnsB5 have transmembrane domains, whereas PnsB1, PnsB2, and PnsB3 are localized to the stroma side, probably anchored on PnsB4 and PnsB5. Although the molecular function of subcomplex B remains unelucidated, defects in its subunits result in the destabilization of the total complex. Subcomplex L contains at least five subunits (PnsL1-5) and is also specific to chloroplast NDH-1. Phylogenetically, the occurrence of subcomplex L is linked to the formation of a supercomplex between NDH-1 and PSI. Three of the subcomplex L subunits (PnsL1-3) show sequence similarities to lumenal subunits of PSII: PnsL1 is PsbP-like protein 2 (PPL2), and PnsL2 and PnsL3 are forms of PsbQ-like protein (PQL). In PSII, PsbP and PsbQ stabilize the PSII supercomplex by interacting with CP26 and CP47, supporting the idea that subcomplex L stabilizes the NDH-1-PSI supercomplex at the lumen side. Three subunits of subcomplex ED - NdhS, NdhT, and NdhU - have been identified by proteomic analysis of the NDH-1-PSI supercomplex. NdhS is involved in ferredoxin (Fd) binding. NdhT and NdhU are J and J-like proteins, respectively, that have a transmembrane domain and likely form a heterodimer required for stabilizing NdhS. NdhV is a subunit loosely bound to subcomplex ED, forming the most fragile part of the complex. Subcomplex ED interacts with subcomplex A to form the Fd-binding site, which includes the Fd-oxidizing site | Arabidopsis thaliana |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| NDH-1 | - |
Nicotiana tabacum |
| NDH-1 | - |
Arabidopsis thaliana |
| NDH-1 | - |
Physcomitrium patens |
| NDH-1 | - |
Marchantia polymorpha |
| NDH-1 | - |
Synechocystis sp. PCC 6803 |
| NDH-1 | - |
Thermosynechococcus vestitus |
| type I NADH dehydrogenase | - |
Nicotiana tabacum |
| type I NADH dehydrogenase | - |
Arabidopsis thaliana |
| type I NADH dehydrogenase | - |
Physcomitrium patens |
| type I NADH dehydrogenase | - |
Marchantia polymorpha |
| type I NADH dehydrogenase | - |
Synechocystis sp. PCC 6803 |
| type I NADH dehydrogenase | - |
Thermosynechococcus vestitus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| Ferredoxin | both chloroplast and cyanobacterial NDH-1s oxidize reduced ferredoxin. Subunit NdhS is involved in ferredoxin (Fd) binding. NdhT and NdhU are J and J-like proteins, respectively, that have a transmembrane domain and likely form a heterodimer required for stabilizing NdhS. NdhV is a subunit loosely bound to subcomplex ED, forming the most fragile part of the complex. Subcomplex ED interacts with subcomplex A to form the Fd-binding site, which includes the Fd-oxidizing site | Nicotiana tabacum | |
| Ferredoxin | both chloroplast and cyanobacterial NDH-1s oxidize reduced ferredoxin. Subunit NdhS is involved in ferredoxin (Fd) binding. NdhT and NdhU are J and J-like proteins, respectively, that have a transmembrane domain and likely form a heterodimer required for stabilizing NdhS. NdhV is a subunit loosely bound to subcomplex ED, forming the most fragile part of the complex. Subcomplex ED interacts with subcomplex A to form the Fd-binding site, which includes the Fd-oxidizing site | Arabidopsis thaliana | |
| Ferredoxin | both chloroplast and cyanobacterial NDH-1s oxidize reduced ferredoxin. Subunit NdhS is involved in ferredoxin (Fd) binding. NdhT and NdhU are J and J-like proteins, respectively, that have a transmembrane domain and likely form a heterodimer required for stabilizing NdhS. NdhV is a subunit loosely bound to subcomplex ED, forming the most fragile part of the complex. Subcomplex ED interacts with subcomplex A to form the Fd-binding site, which includes the Fd-oxidizing site | Physcomitrium patens | |
| Ferredoxin | both chloroplast and cyanobacterial NDH-1s oxidize reduced ferredoxin. Subunit NdhS is involved in ferredoxin (Fd) binding. NdhT and NdhU are J and J-like proteins, respectively, that have a transmembrane domain and likely form a heterodimer required for stabilizing NdhS. NdhV is a subunit loosely bound to subcomplex ED, forming the most fragile part of the complex. Subcomplex ED interacts with subcomplex A to form the Fd-binding site, which includes the Fd-oxidizing site | Marchantia polymorpha | |
| Ferredoxin | both chloroplast and cyanobacterial NDH-1s oxidize reduced ferredoxin. The NdhS subunit of the hydrophilic domain of NDH-1M is essential for binding of Fd, the putative electron donor to cyanobacterial NDH-1 complexes | Synechocystis sp. PCC 6803 | |
| Ferredoxin | both chloroplast and cyanobacterial NDH-1s oxidize reduced ferredoxin. The NdhS subunit of the hydrophilic domain of NDH-1M is essential for binding of Fd, the putative electron donor to cyanobacterial NDH-1 complexes | Thermosynechococcus vestitus | |
| plastoquinone | - |
Nicotiana tabacum | |
| plastoquinone | - |
Arabidopsis thaliana | |
| plastoquinone | - |
Physcomitrium patens | |
| plastoquinone | - |
Marchantia polymorpha | |
| plastoquinone | - |
Synechocystis sp. PCC 6803 | |
| plastoquinone | - |
Thermosynechococcus vestitus | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | co-evolution of NDH-1 and NDH-2 in the green lineage. Evolution of NDH-1-related protein complexes, overview | Arabidopsis thaliana |
| evolution | coevolution of NDH-1 and NDH-2 in the green lineage. Evolution of NDH-1-related protein complexes, overview | Nicotiana tabacum |
| evolution | coevolution of NDH-1 and NDH-2 in the green lineage. Evolution of NDH-1-related protein complexes, overview | Physcomitrium patens |
| evolution | coevolution of NDH-1 and NDH-2 in the green lineage. Evolution of NDH-1-related protein complexes, overview | Marchantia polymorpha |
| evolution | in addition to the NDH-1M module, which is common to all complexes, cyanobacterial NDH-1 complexes differ in the nature of the NdhD and NdhF subunits. Evolution of NDH-1-related protein complexes, overview | Thermosynechococcus vestitus |
| evolution | in addition to the NDH-1M module, which is common to all complexes, cyanobacterial NDH-1 complexes differ in the nature of the NdhD and NdhF subunits. The Synechocystis sp. PCC6803 genome contains six different ndhD genes (ndhD1-6) and three different ndhF genes (ndhF1, ndhF3, and ndhF4). Evolution of NDH-1-related protein complexes, overview | Synechocystis sp. PCC 6803 |
| metabolism | biochemical composition and activity of NDH-1 in relation to the physiology and regulation of photosynthesis, particularly focusing on their roles in cyclic electron flow around PSI, chlororespiration, and acclimation to changing environments, comparison to NDH-2. Metabolic and physiological functions of NDH-1, regulation of NDH-1, overview | Synechocystis sp. PCC 6803 |
| metabolism | biochemical composition and activity of NDH-1 in relation to the physiology and regulation of photosynthesis, particularly focusing on their roles in cyclic electron flow around PSI, chlororespiration, and acclimation to changing environments, comparison to NDH-2. Metabolic and physiological functions of NDH-1, regulation of NDH-1, overview | Thermosynechococcus vestitus |
| metabolism | the biogenesis of PSII and NDH-1 plastidial complexes shows some similarity. Biochemical composition and activity of NDH-1 in relation to the physiology and regulation of photosynthesis, particularly focusing on their roles in cyclic electron flow around PSI, chlororespiration, and acclimation to changing environments, comparison to NDH-2. Metabolic and physiological functions of NDH-1, regulation of NDH-1, overview. Involvement of NDH-1 in a supercomplex with photosystem I | Nicotiana tabacum |
| metabolism | the biogenesis of PSII and NDH-1 plastidial complexes shows some similarity. Biochemical composition and activity of NDH-1 in relation to the physiology and regulation of photosynthesis, particularly focusing on their roles in cyclic electron flow around PSI, chlororespiration, and acclimation to changing environments, comparison to NDH-2. Metabolic and physiological functions of NDH-1, regulation of NDH-1, overview. Involvement of NDH-1 in a supercomplex with photosystem I | Physcomitrium patens |
| metabolism | the biogenesis of PSII and NDH-1 plastidial complexes shows some similarity. Biochemical composition and activity of NDH-1 in relation to the physiology and regulation of photosynthesis, particularly focusing on their roles in cyclic electron flow around PSI, chlororespiration, and acclimation to changing environments, comparison to NDH-2. Metabolic and physiological functions of NDH-1, regulation of NDH-1, overview. Involvement of NDH-1 in a supercomplex with photosystem I | Marchantia polymorpha |
| metabolism | the biogenesis of PSII and NDH-1 plastidial complexes shows some similarity. Two closely related Arabidopsis thaliana proteins, photosynthese-affected-mutant 68 (PAM68) and PAM68-LIKE (PAM68L), are involved in the assembly of the PSII core and of the membrane part of chloroplast NDH-1, respectively. Biochemical composition and activity of NDH-1 in relation to the physiology and regulation of photosynthesis, particularly focusing on their roles in cyclic electron flow around PSI, chlororespiration, and acclimation to changing environments, comparison to NDH-2. Metabolic and physiological functions of NDH-1, regulation of NDH-1, overview. Involvement of NDH-1 in a supercomplex with photosystem I | Arabidopsis thaliana |
| physiological function | 16 of the 34 editing sites in the Arabidopsis thaliana plastid genome are associated with four ndh genes (ndhB, ndhD, ndhF, and ndhG). Metabolic and physiological functions of NDH-1, overview. In Arabidopsis thaliana ruptured chloroplasts, NADPH-dependent plastoquinone (PQ) reduction by the NDH-1 complex is strictly dependent on the presence of ferredoxin (Fd) | Arabidopsis thaliana |
| physiological function | metabolic and physiological functions of NDH-1, overview | Nicotiana tabacum |
| physiological function | metabolic and physiological functions of NDH-1, overview | Physcomitrium patens |
| physiological function | metabolic and physiological functions of NDH-1, overview | Marchantia polymorpha |
| physiological function | metabolic and physiological functions of NDH-1, overview | Synechocystis sp. PCC 6803 |
| physiological function | metabolic and physiological functions of NDH-1, overview | Thermosynechococcus vestitus |
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