Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

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

Protein Variants

EC Number Protein Variants Comment Organism
7.1.1.10 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

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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
7.1.1.10 450000
-
about, complex NDH-1L, MALDI-TOF mass spectrometry Thermosynechococcus vestitus

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

Organism

EC Number Organism UniProt Comment Textmining
7.1.1.10 Thermosynechococcus vestitus Q8DKZ3
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
7.1.1.10 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)

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

Subunits

EC Number Subunits Comment Organism
7.1.1.10 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

EC Number Synonyms Comment Organism
7.1.1.10 NDH-1L complex
-
Thermosynechococcus vestitus
7.1.1.10 NdhL
-
Thermosynechococcus vestitus

Cofactor

EC Number Cofactor Comment Organism Structure
7.1.1.10 Ferredoxin
-
Thermosynechococcus vestitus
7.1.1.10 plastoquinone
-
Thermosynechococcus vestitus