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chlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
protochlorophyllide + oxidized ferredoxin + 2 ADP + 2 phosphate + 2 H+
chlorophyllide a + reduced ferredoxin + ATP
protochlorophyllide + oxidized ferredoxin + ADP + phosphate
protochlorophyllide + oxidized ferredoxin + ADP + phosphate
chlorophyllide a + reduced ferredoxin + ATP
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
protochlorophyllide a + reduced ferredoxin + 4 ATP + 4 H2O
chlorophyllide a + oxidized ferredoxin + 4 ADP + 4 phosphate
additional information
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chlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
protochlorophyllide + oxidized ferredoxin + 2 ADP + 2 phosphate + 2 H+
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chlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
protochlorophyllide + oxidized ferredoxin + 2 ADP + 2 phosphate + 2 H+
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chlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
protochlorophyllide + oxidized ferredoxin + 2 ADP + 2 phosphate + 2 H+
Thermosynechococcus vestitus
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chlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
protochlorophyllide + oxidized ferredoxin + 2 ADP + 2 phosphate + 2 H+
Thermosynechococcus vestitus
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ferredoxin provides a single electron to ChlL2, which in turn transfers an electron to (ChlN/ChlB)2. Hydrolysis of the two ATP molecules results in the dissociation of ChlL2 from reduced (ChlN/ChlB)2. Protochlorophyllide reduction is completed after two sequential catalytic redox cycles. Substrate recognition by (ChlN/ChlB)2 essentially involves all functional groups of the substrate, modeling of the substrate binding site of (ChlN/ChlB)2, overview. Electron transfer pathway via the various redox centers of DPOR to the substrate, overview
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chlorophyllide a + reduced ferredoxin + ATP
protochlorophyllide + oxidized ferredoxin + ADP + phosphate
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chlorophyllide a + reduced ferredoxin + ATP
protochlorophyllide + oxidized ferredoxin + ADP + phosphate
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chlorophyllide a + reduced ferredoxin + ATP
protochlorophyllide + oxidized ferredoxin + ADP + phosphate
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protochlorophyllide + oxidized ferredoxin + ADP + phosphate
chlorophyllide a + reduced ferredoxin + ATP
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protochlorophyllide + oxidized ferredoxin + ADP + phosphate
chlorophyllide a + reduced ferredoxin + ATP
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protochlorophyllide + oxidized ferredoxin + ADP + phosphate
chlorophyllide a + reduced ferredoxin + ATP
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protochlorophyllide + oxidized ferredoxin + ADP + phosphate
chlorophyllide a + reduced ferredoxin + ATP
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protochlorophyllide + oxidized ferredoxin + ADP + phosphate
chlorophyllide a + reduced ferredoxin + ATP
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protochlorophyllide + oxidized ferredoxin + ADP + phosphate
chlorophyllide a + reduced ferredoxin + ATP
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DPOR catalyzes the stereo-specific reduction of C17-C18 double bond on the D-ring of protochlorophyllide
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protochlorophyllide + oxidized ferredoxin + ADP + phosphate
chlorophyllide a + reduced ferredoxin + ATP
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protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
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protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
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protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
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protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
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protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
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protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
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protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
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protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
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protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
DPOR catalyzes the formation of chlorophyllide a through ATP-dependent, stereospecific reduction of the C-17=C-18 double bond of Pchlide ring D
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protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
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the homodimeric ChlL2 subunit carrying a [4Fe-4S] cluster transfers electrons to the corresponding heterotetrameric catalytic subunit (ChlN/ChlB)2, which also possesses a redox active [4Fe-4S] cluster
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protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
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protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
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protochlorophyllide a + reduced ferredoxin + 4 ATP + 4 H2O
chlorophyllide a + oxidized ferredoxin + 4 ADP + 4 phosphate
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protochlorophyllide a + reduced ferredoxin + 4 ATP + 4 H2O
chlorophyllide a + oxidized ferredoxin + 4 ADP + 4 phosphate
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additional information
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proposed catalytic redox cycle of DPOR, overview
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additional information
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although chlorophyllide c binds to the substrate-binding pocket in the NB-protein, the C17-C18 double bond on the D-ring of chlorophyllide c is not reduced by the DPOR
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additional information
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DPOR is a nitrogenase-like enzyme consisting of two components, L-protein (a BchL dimer) and NB-protein (a BchN-BchB heterotetramer)
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additional information
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each catalytic BchN-BchB unit contains one protochlorophyllidee 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 protochlorophyllid and an aspartate from BchB serve as proton donors for C18 and C17 of protochlorophyllide, respectively, overview
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additional information
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the C175C18 double bond of chlorophyll c is not reduced by DPOR
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additional information
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The reaction mechanism begins with single-electron reduction of the substrate by the (Cys)3Asp-ligated [4Fe-4S]-center, yielding a negatively-charged intermediate. Depending on the rate of Fe-S cluster re-reduction, the reaction either proceeds through double protonation of the single-electron-reduced substrate, or by alternating proton/electron transfer. The Fe-S cluster rereduction should be the rate-limiting stage of the process
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additional information
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The reaction mechanism begins with single-electron reduction of the substrate by the (Cys)3Asp-ligated [4Fe-4S]-center, yielding a negatively-charged intermediate. Depending on the rate of Fe-S cluster re-reduction, the reaction either proceeds through double protonation of the single-electron-reduced substrate, or by alternating proton/electron transfer. The Fe-S cluster rereduction should be the rate-limiting stage of the process
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additional information
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DPOR is a nitrogenase-like enzyme consisting of two components, L-protein (a BchL dimer) and NB-protein (a BchN-BchB heterotetramer)
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additional information
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each catalytic BchN-BchB unit contains one protochlorophyllidee 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 protochlorophyllid and an aspartate from BchB serve as proton donors for C18 and C17 of protochlorophyllide, respectively, overview
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additional information
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the C175C18 double bond of chlorophyll c is not reduced by DPOR
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additional information
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Thermosynechococcus vestitus
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the invitro assay is performed with purified recombinant GST-tagged (ChlN/ChlB)2 complex and a ChlL2 subunit purified from Prochlorococcus marinus
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