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heterodimer
1 * 38000 + 1 * 49000 + 1 * 58000, SDS-PAGE
heterooctamer
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(alpha2)2(betagamma)4, DPOR is a nitrogenase-like enzyme consisting of two components, L-protein, a BchL dimer, and NB-protein, a BchN-BchB heterotetramer, which are structurally related to nitrogenase Fe protein and MoFe protein, respectively
heterooctamer
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(alpha2)2(betagamma)4, DPOR is a nitrogenase-like enzyme consisting of two components, L-protein, a BchL dimer, and NB-protein, a BchN-BchB heterotetramer, which are structurally related to nitrogenase Fe protein and MoFe protein, respectively
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heterooctamer
Thermosynechococcus vestitus
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(alpha2)2(betagamma)4, DPOR is composed of the subunits ChlL, ChlN, and ChlB. Homodimeric ChlL2 bearing an intersubunit [4Fe-4S] cluster is an ATP-dependent reductase transferring single electrons to the heterotetrameric (ChlN/ChlB)2 complex. The latter contains two intersubunit [4Fe-4S] clusters and two protochlorophyllide binding sites, respectively, structure analysis of the catalytic (ChlN/ChlB)2 complex, overview. Subunits ChlN and ChlB exhibit a related architecture of three subdomains each built around a central, parallel beta-sheet surrounded by alpha-helices. Two ChlL2 dimers simultaneously interact with the (ChlN/ChlB)2 tetramer, giving rise to a heterooctameric holoenzyme
heterotetramer
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2 * 48671 + 2 * 57191, subunit BchN and subunit BchB, calculated from amino acid sequence
heterotetramer
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2 * 51000 + 2 * 43000 , NB-protein of DPOR, SDS-PAGE
heterotetramer
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2 * 52000 + 2 * 60000, NB-protein complex, SDS-PAGE
heterotetramer
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2 * 57191 + 2 * 46038, NB-protein of DPOR, calculated from amino acid sequence
homodimer
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2 * 31000, L-protein of DPOR, SDS-PAGE
homodimer
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2 * 33413, L-protein of DPOR, calculated from amino acid sequence
homodimer
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2 * 36000, S-tag subunit BchL, SDS-PAGE
homodimer
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2 * 36046, subunit BchL calculated from amino acid sequence
octamer
(L2)2(NB)2 enzyme complex with perfect symmetry. Subunits L2 and NifH2 both contain a subunit-bridging [4Fe-4S] cluster, whereas the [4Fe-4S] cluster at the N/B subunit interface of (NB)2 is located in an analogous position as the [8Fe-7S] P-cluster at the NifD/NifK subunit interface of (NifDK)2
octamer
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octameric (ChlN/ChlB)2(ChlL2)2 subunit complex, 4 * 35000, subunit ChlL, + 2 * 45000, subunit ChlN, 2 * 60000, subunit ChlB, SDS-PAGE, 4 * 32395,subunit ChlL, + 2 * 46199, subunit ChlN, 2 * 58729, subunit ChlB, sequence calculation
octamer
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octameric (ChlN/ChlB)2(ChlL2)2 subunit complex, with homodimeric subunit ChlL2 and heterotetrameric catalytic subunit (ChlN/ChlB)2
additional information
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DPOR consists of two components: a reductase component designated L-protein (a BchL dimer) and a catalytic component named NB-protein (a BchNBchB heterotetramer), structure analysis and comparison to the nitrogenase complex, overview
additional information
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DPOR consists of two components: a reductase component designated L-protein (a BchL dimer) and a catalytic component named NB-protein (a BchN-BchB heterotetramer), structure analysis and comparison to the nitrogenase complex, overview
additional information
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DPOR consists of two components: a reductase component designated L-protein (a BchL dimer) and a catalytic component named NB-protein (a BchN-BchB heterotetramer), structure analysis and comparison to the nitrogenase complex, overview
additional information
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DPOR consists of two components: a reductase component designated L-protein (a BchL dimer) and a catalytic component named NB-protein (a BchN-BchB heterotetramer), structure analysis and comparison to the nitrogenase complex, overview
additional information
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the light-independent enzyme consists of three subunit types, ChlL, ChlN and ChlB. ChlB in photosynthetic bacteria and plastids is the major subunit that catalyzes the reduction of protochlorophyllide to chlorophyllide
additional information
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DPOR consists of two components: a reductase component designated L-protein (a BchL dimer) and a catalytic component named NB-protein (a BchN-BchB heterotetramer), structure analysis and comparison to the nitrogenase complex, overview
additional information
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each catalytic BchN-BchB unit contains one protochlorophyllide and one iron-sulfur NB-cluster coordinated uniquely by one aspartate and three cysteines. Unique aspartate ligation is not necessarily needed for the cluster assembly but is essential for the catalytic activity. Specific protochlorophyllide-binding accompanies the partial unwinding of an alpha-helix that belongs to the next catalytic BchN-BchB unit, unique trans-specific reduction mechanism in which the distorted C17-propionate of protochlorophyllide and an aspartate from BchB serve as proton donors for C18 and C17 of protochlorophyllide, respectively, overview
additional information
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DPOR consists of two components: a reductase component designated L-protein (a BchL dimer) and a catalytic component named NB-protein (a BchN-BchB heterotetramer), structure analysis and comparison to the nitrogenase complex, overview. The NB-cluster is unique because it is coordinated by three Cys residues from BchN (BchN-Cys26, BchN-Cys51, BchN-Cys112) and one Asp residue from BchB (BchB-Asp36)
additional information
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each catalytic BchN-BchB unit contains one protochlorophyllide and one iron-sulfur NB-cluster coordinated uniquely by one aspartate and three cysteines. Unique aspartate ligation is not necessarily needed for the cluster assembly but is essential for the catalytic activity. Specific protochlorophyllide-binding accompanies the partial unwinding of an alpha-helix that belongs to the next catalytic BchN-BchB unit, unique trans-specific reduction mechanism in which the distorted C17-propionate of protochlorophyllide and an aspartate from BchB serve as proton donors for C18 and C17 of protochlorophyllide, respectively, overview
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additional information
Thermosynechococcus vestitus
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model of the complete hetero-octameric DPOR and distance between cofactors, overview