Literature summary for 7.1.1.10 extracted from

Pan, X.; Cao, D.; Xie, F.; Xu, F.; Su, X.; Mi, H.; Zhang, X.; Li, M.
Structural basis for electron transport mechanism of complex I-like photosynthetic NAD(P)H dehydrogenase (2020), Nat. Commun., 11, 610 .

Search for more literature for 7.1.1.10

Cloned(Commentary)

Cloned (Comment)	Organism
gene ndhS , recombinant expression of two NDH-1L subunits, NdhS and ferredoxin	Thermosynechococcus vestitus

Protein Variants

Protein Variants	Comment	Organism
additional information	preparation of NDH-Fd supercomplex: the purified NDH-1L complex is concentrated to 1 mg/ml and mixed with NdhS, NdhV, and Fd proteins. The molar ratio of NDH-1L:NdhS:NdhV:Fd is set to 1:4:6:6. The mixture is incubated for 1 h at 20°C and then concentrated to 12 mg/ml	Thermosynechococcus vestitus

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
thylakoid membrane	the NDH-1L is more rigid in the membrane arm at low pH, whereas the complex is more strongly associated between its two arms at higher pH	Thermosynechococcus vestitus	42651	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Fe2+	bound in [4Fe-4S] clusters and ferredoxin	Thermosynechococcus vestitus

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

Organism

Organism	UniProt	Comment	Textmining
Thermosynechococcus vestitus	Q8DKZ3	-	-

Purification (Commentary)

Purification (Comment)	Organism
native NDH-1L complex from strain BP-1 by membrane preparation through ultracentrifugation at 150000 x g, nickel affinity chromatography (owing to the native histidine-rich area within the hydrophobic subunit NdhF1), and solubilization with 1% w/v n-dodecyl-beta-D-maltoside, followed by again nickel affinity chromatography, ultrafiltration, and gel filtration	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]	-	Thermosynechococcus vestitus	2 oxidized ferredoxin [iron-sulfur] cluster + plastoquinol + 7 H+[side 2]	-	?
2 reduced ferredoxin [iron-sulfur] cluster + plastoquinone + 6 H+[side 1]	analysis of binding manner of NDH-1L with Fd and PQ, binding structures, overview	Thermosynechococcus vestitus	2 oxidized ferredoxin [iron-sulfur] cluster + plastoquinol + 7 H+[side 2]	-	?
additional information	the ferredoxin (Fd) binding pocket is mainly formed by subunits NdhI and NdhH, structure overview. Fd and NdhV almost symmetrically bind the hairpin loop of NdhI from the opposite sides	Thermosynechococcus vestitus	?	-	-

Subunits

Subunits	Comment	Organism
More	two structures of NDH-1L from Thermosynechococcus elongatus strain BP-1, in complex with one ferredoxin (Fd) and an endogenous plastoquinone (PQ), respectively. Comparison of NDH-PQ structure (NDHpH7) with previously reported two NDH-1L structures NDHpH6 and NDHpH8 (PDB IDs 6NBY and 6HUM) superposed on NdhA subunit, overview	Thermosynechococcus vestitus

Synonyms

Synonyms	Comment	Organism
NAD(P)H dehydrogenase-like (NDH) complex	-	Thermosynechococcus vestitus
NDH-1L	-	Thermosynechococcus vestitus
NdhL	-	Thermosynechococcus vestitus

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Thermosynechococcus vestitus

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7	8	-	Thermosynechococcus vestitus

pH Range

pH Minimum	pH Maximum	Comment	Organism
additional information	-	comparison of NDH-PQ structure (NDHpH7) with previously reported two NDH-1L structures NDHpH6 and NDHpH8 (PDB IDs 6NBY and 6HUM) superposed on NdhA subunit, overview	Thermosynechococcus vestitus
6	9	highly reduced activity at pH 6.0 and pH 9.0, maximal activity at pH 7.0-8.0	Thermosynechococcus vestitus

Cofactor

Cofactor	Comment	Organism	Structure
Ferredoxin	-	Thermosynechococcus vestitus
plastoquinone	-	Thermosynechococcus vestitus
[4Fe-4S] cluster	-	Thermosynechococcus vestitus

General Information

General Information	Comment	Organism
additional information	NDH-1L structure modeling, structure-function analysis, overview. Analysis of the binding manner of NDH-1L with Fd and PQ, as well as the structural elements crucial for proper functioning of the NDH-1L complex. The hydrophilic arm contains nine NDH subunits, including NdhV and the [4Fe-4S] clusters, the NDH-1L is more rigid in the membrane arm at low pH, whereas the complex is more strongly associated between its two arms at higher pH. NdhV is composed of central loops/beta-strands, which is flanked by the N- and C-terminal helix at one side. In the NDH-Fd structure, NdhV is located above NdhN and NdhS. The central loops/beta-strands of NdhV join with the loops/beta-strands of NdhS, forming strong interactions. In NDH complex, the soluble subunits NdhK and NdhH together with the membrane subunit NdhA play major role in maintaining the association between the membrane and hydrophilic arms. In addition, NdhI, NdhC, and the OPS subunit NdhL also contribute to the interaction between the two arms. The cytoplasmic loop between the first and second TMH (TMH1-2 loop) of NdhC contacts NdhA and the soluble subunits NdhK/NdhH/NdhM, reinforcing the interactions between the two arms. Moreover, the membrane subunit NdhL has a C-terminal fragment projecting into the cytoplasmic region and associating with NdhI/NdhN. While the soluble NdhI possesses an N-terminal amphiphilic helix (N-helix) that embraces the membrane subunits NdhA/NdhL. In addition, three lipid molecules are found at the interface between the two arms, facilitating their association. Two of these lipids link the N-helix of NdhI with the membrane domain of NdhA and NdhC, whereas the third lipid is located in an enclosed cavity formed by the N-terminal fragments from NdhL, NdhN, and NdhK. Pivotal role of lipid molecules in connecting the hydrophilic arm with the membrane arm of the NDH complex	Thermosynechococcus vestitus
physiological function	NAD(P)H dehydrogenase-like (NDH) complex NDH-1L of cyanobacteria plays a crucial role in cyclic electron flow (CEF) around photosystem I and respiration processes. NDH-1L couples the electron transport from ferredoxin (Fd) to plastoquinone (PQ) and proton pumping from cytoplasm to the lumen that drives the ATP production. NDH-1L-dependent CEF increases the ATP/NADPH ratio, and is therefore pivotal for oxygenic phototrophs to function under stress	Thermosynechococcus vestitus

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Release 2023.1 (January 2023)