Literature summary for 7.1.1.10 extracted from

Zhang, P.; Battchikova, N.; Paakkarinen, V.; Katoh, H.; Iwai, M.; Ikeuchi, M.; Pakrasi, H.B.; Ogawa, T.; Aro, E.M.
Isolation, subunit composition and interaction of the NDH-1 complexes from Thermosynechococcus elongatus BP-1 (2005), Biochem. J., 390, 513-520 .

Search for more literature for 7.1.1.10

Cloned(Commentary)

Cloned (Comment)	Organism
gene ndhL, recombinant expression of HIs-tagged enzyme complex in Thermosynechococcus elongatus	Thermosynechococcus vestitus

Protein Variants

Protein Variants	Comment	Organism
additional information	several strains of Thermosynechococcus elongatus are constructed by adding a His-tag to different subunits of NDH-1. Two strains with His-tag on CupA and NdhL are successfully used to isolate NDH-1 complexes by one-step Ni2+ column chromatography, revealing the presence of three complexes with molecular masses of about 450, 300 and 190 kDa, which are identified by MS to be NDH-1L, NDH-1M and NDH-1S respectively. A larger complex of about 490 kDa is also isolated from the NdhL-His strain. This complex, designated NDH-1MS, is composed of NDH-1M and NDH-1S (EC 7.1.1.11). Selection of the subunit for His tagging is crucial for isolation of NDH-1 complexes	Thermosynechococcus vestitus

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
thylakoid membrane	-	Thermosynechococcus vestitus	42651	-

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
450000	-	about, complex NDH-1L, MALDI-TOF mass spectrometry	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
wild-type NDH-1L complex is recovered from wild-type cells of Thermosynechococcus elongatus by Ni2+ column chromatography, NDH-1S or NDH-1M is not recovered from wild-type cells by chromatography of this kind, recombinant His-tagged enzyme complex NDH-1L from Thermosynechococcus elongatus solubilized thylakoid membranes by nickel affinity chromatography	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]	-	?

Subunits

Subunits	Comment	Organism
More	several strains of Thermosynechococcus elongatus are constructed by adding a His-tag to different subunits of NDH-1. Two strains with His-tag on CupA and NdhL are successfully used to isolate NDH-1 complexes by one-step Ni2+ column chromatography, revealing the presence of three complexes with molecular masses of about 450, 300 and 190 kDa, which are identified by MS to be NDH-1L, NDH-1M and NDH-1S respectively. A larger complex of about 490 kDa is also isolated from the NdhL-His strain. This complex, designated NDH-1MS, is composed of NDH-1M and NDH-1S (EC 7.1.1.11). The NDH-1L complex is recovered from wild-type cells of Thermosynechococcus elongatus by Ni2+ column chromatography. NdhF1 subunit present only in NDH-1L has a sequence of -HHDHHSHH- internally, which appears to have an affinity for the Ni2+ column. NDH-1S or NDH-1M are not recovered from wild-type cells by chromatography of this kind. The BN/SDS/PAGE analysis of membranes solubilized by a low concentration of detergent indicated the presence of abundant NDH-1MS, but not NDH-1M or NDH-1S. Thus, NDH-1S is associated with NDH-1M in vivo. Selection of the subunit for His tagging is crucial for isolation of NDH-1 complexes	Thermosynechococcus vestitus

Synonyms

Synonyms	Comment	Organism
NDH-1L complex	-	Thermosynechococcus vestitus
NdhL	-	Thermosynechococcus vestitus

Cofactor

Cofactor	Comment	Organism	Structure
Ferredoxin	-	Thermosynechococcus vestitus
plastoquinone	-	Thermosynechococcus vestitus

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Release 2023.1 (January 2023)