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3,8-divinyl chlorophyll a + reduced ferredoxin [iron-sulfur] cluster + H+
chlorophyll a + oxidized ferredoxin [iron-sulfur] cluster
-
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-
?
3,8-divinyl chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
chlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
3,8-divinyl chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + NADPH + H+
chlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + NADP+
preferred substrate
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-
?
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+ + NADPH + H+
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + NADP+
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + NADPH + H+
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + NADP+
8-vinyl protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
-
-
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-
?
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
protochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
8-vinyl protochlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
-
-
-
-
?
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
additional information
?
-
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+ + NADPH + H+
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + NADP+
-
-
-
?
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+ + NADPH + H+
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + NADP+
-
-
-
?
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + NADPH + H+
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + NADP+
-
-
-
?
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + NADPH + H+
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + NADP+
-
-
-
?
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + NADPH + H+
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + NADP+
is reduced only under conditions in which this pigment accumulates as a result of perturbed formation of chlorophyllide
-
-
?
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
-
-
-
?
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
-
-
-
?
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
-
-
-
-
?
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
-
-
-
?
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
-
-
-
-
?
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
-
-
-
-
?
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
-
-
-
-
?
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
-
-
-
-
?
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
-
-
-
-
?
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
-
-
-
-
?
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
-
-
-
-
?
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
-
-
-
-
?
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
-
-
-
-
?
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
-
-
-
-
?
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
-
-
-
-
?
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
-
-
-
-
?
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
-
-
-
-
?
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
-
-
-
-
?
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
-
-
-
-
?
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
-
-
-
-
?
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
-
-
-
?
additional information
?
-
using electrons provided by reduced ferredoxin or dithionite, recombinant BciB is active and reduced the 8-vinyl moiety of the substrate, 8-vinyl protochlorophyllide, producing protochlorophyllide a. BciB requires an additional electron donor, ferredoxin, together with NADPH
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-
?
additional information
?
-
-
using electrons provided by reduced ferredoxin or dithionite, recombinant BciB is active and reduced the 8-vinyl moiety of the substrate, 8-vinyl protochlorophyllide, producing protochlorophyllide a. BciB requires an additional electron donor, ferredoxin, together with NADPH
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-
?
additional information
?
-
using electrons provided by reduced ferredoxin or dithionite, recombinant BciB is active and reduced the 8-vinyl moiety of the substrate, 8-vinyl protochlorophyllide, producing protochlorophyllide a. BciB requires an additional electron donor, ferredoxin, together with NADPH
-
-
?
additional information
?
-
although the native BciB is able to reduce the 8V group of Pchlide, the preferred substrate for this enzyme is 8V Chlide, with only a small amount of 8E Pchlide detected in the wild-type when grown under pigment accumulating conditions
-
-
?
additional information
?
-
cyanobacterial 3,8-divinyl chlorophyllide reductase (DVR) is a Chl biosynthetic enzyme that has many promiscuous activities besides the 3,8-divinyl chlorophyllide reductase activity, e.g. 7-hydroxymethyl chlorophyll a reductase activity. The Chl c2 to Chl c1 conversion is existent in cyanobacteria as a promiscuous activity of F-DVR. Chl c1 is synthesized by the reduction of the 8-vinyl group of Chl c2 or Chl c1 is synthesized from monovinyl-protochlorophyllide by the dehydrogenase
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-
?
additional information
?
-
substrate specificity, overview. Cyanobacterial F-DVR exhibits a broad substrate specificity and converts 3,8-divinylprotochlorophyllide a, 3,8-divinyl chlorophyllide a, and 3,8-divinyl chlorophyll a to the respective monovinyl molecules. When 7-hydroxymethyl chlorophyllide (HMChlide) a is incubated with F-DVR, chlorophyllide a is generated
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-
?
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3,8-divinyl chlorophyll a + reduced ferredoxin [iron-sulfur] cluster + H+
chlorophyll a + oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
3,8-divinyl chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
chlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
3,8-divinyl chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + NADPH + H+
chlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + NADP+
preferred substrate
-
-
?
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+ + NADPH + H+
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + NADP+
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + NADPH + H+
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + NADP+
8-vinyl protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
-
-
-
-
?
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
protochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
8-vinyl protochlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
-
-
-
-
?
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
additional information
?
-
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+ + NADPH + H+
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + NADP+
-
-
-
?
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+ + NADPH + H+
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + NADP+
-
-
-
?
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + NADPH + H+
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + NADP+
-
-
-
?
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + NADPH + H+
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + NADP+
-
-
-
?
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + NADPH + H+
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + NADP+
is reduced only under conditions in which this pigment accumulates as a result of perturbed formation of chlorophyllide
-
-
?
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
-
-
-
?
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
-
-
-
?
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
-
-
-
-
?
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
-
-
-
?
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
-
-
-
-
?
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
-
-
-
-
?
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
-
-
-
-
?
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
-
-
-
-
?
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
-
-
-
-
?
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
-
-
-
-
?
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
-
-
-
-
?
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
-
-
-
-
?
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
-
-
-
-
?
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
-
-
-
-
?
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
-
-
-
-
?
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
-
-
-
-
?
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
-
-
-
-
?
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
-
-
-
-
?
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
-
-
-
-
?
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
-
-
-
-
?
protochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster
3,8-divinyl protochlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + H+
-
-
-
?
additional information
?
-
although the native BciB is able to reduce the 8V group of Pchlide, the preferred substrate for this enzyme is 8V Chlide, with only a small amount of 8E Pchlide detected in the wild-type when grown under pigment accumulating conditions
-
-
?
additional information
?
-
cyanobacterial 3,8-divinyl chlorophyllide reductase (DVR) is a Chl biosynthetic enzyme that has many promiscuous activities besides the 3,8-divinyl chlorophyllide reductase activity, e.g. 7-hydroxymethyl chlorophyll a reductase activity. The Chl c2 to Chl c1 conversion is existent in cyanobacteria as a promiscuous activity of F-DVR. Chl c1 is synthesized by the reduction of the 8-vinyl group of Chl c2 or Chl c1 is synthesized from monovinyl-protochlorophyllide by the dehydrogenase
-
-
?
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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evolution
either F-DVR or N-DVR is found in most photosynthetic organisms, yet both F-DVR and N-DVR exist in the genome of diatoms that contain Chl a and Chl c1
evolution
two unrelated classes of 8-vinyl reductases are known to exist in oxygenic phototrophs, BciA and BciB. Transcript and proteomic analysis of Acaryochloris marina reveal that both bciA and bciB are expressed and their encoded proteins are present in the cell, possibly in order to ensure that all synthesized chlorophyll pigment carries an ethyl group at C-8. The presence of two 8-vinyl reductases is unique for cyanobacteria. The phylogenetic positions of Acaryochloris marina BciA and BciB are both broadly consistent with those shown for Acaryochloris marina in the 16S rRNA trees, suggesting that the bciA and bciB genes have not been acquired by horizontal transfer. However, the positions of Synechococcus spp. in the BciA tree and the clade containing the green sulfur bacteria in the BciB tree are inconsistent with the 16S rRNA phylogeny, indicating that there may have been lateral transfer events during the evolution of both bciA and bciB
evolution
two unrelated classes of C8-vinyl reductase are known to exist, BciA and BciB
evolution
two isozymes of 8-vinyl reductase are described in oxygenic photosynthetic organisms: one encoded by BciA and another by BciB. Only BciB contains an [Fe-S] cluster and most cyanobacteria harbor this form, whereas a few contain BciA. Given this disparity in distribution. Cyanobacterial BciA encodes a functional 8-vinyl reductase, as evidenced by measuring the in vitro activity of recombinant Synechococcus and Acaryochloris BciA. Genomic comparison reveals that BciB had been replaced by BciA during evolution of the marine cyanobacterium Synechococcus, and coincided with replacement of Fe-superoxide dismutase (SOD) with Ni-SOD. These findings imply that the acquisition of BciA confers an adaptive advantage to cyanobacteria living in low-iron oceanic environments
evolution
two isozymes of 8-vinyl reductase are described in oxygenic photosynthetic organisms: one encoded by BciA and another by BciB. Only BciB contains an [Fe-S] cluster and most cyanobacteria harbor this form, whereas a few contain BciA. Given this disparity in distribution. Cyanobacterial BciA encodes a functional 8-vinyl reductase, as evidenced by measuring the in vitro activity of recombinant Synechococcus and Acaryochloris BciA. Genomic comparison reveals that BciB had been replaced by BciA during evolution of the marine cyanobacterium Synechococcus, and coincided with replacement of Fe-superoxide dismutase (SOD) with Ni-SOD. These findings imply that the acquisition of BciA confers an adaptive advantage to cyanobacteria living in low-iron oceanic environments
evolution
-
two unrelated classes of 8-vinyl reductases are known to exist in oxygenic phototrophs, BciA and BciB. Transcript and proteomic analysis of Acaryochloris marina reveal that both bciA and bciB are expressed and their encoded proteins are present in the cell, possibly in order to ensure that all synthesized chlorophyll pigment carries an ethyl group at C-8. The presence of two 8-vinyl reductases is unique for cyanobacteria. The phylogenetic positions of Acaryochloris marina BciA and BciB are both broadly consistent with those shown for Acaryochloris marina in the 16S rRNA trees, suggesting that the bciA and bciB genes have not been acquired by horizontal transfer. However, the positions of Synechococcus spp. in the BciA tree and the clade containing the green sulfur bacteria in the BciB tree are inconsistent with the 16S rRNA phylogeny, indicating that there may have been lateral transfer events during the evolution of both bciA and bciB
-
evolution
-
two isozymes of 8-vinyl reductase are described in oxygenic photosynthetic organisms: one encoded by BciA and another by BciB. Only BciB contains an [Fe-S] cluster and most cyanobacteria harbor this form, whereas a few contain BciA. Given this disparity in distribution. Cyanobacterial BciA encodes a functional 8-vinyl reductase, as evidenced by measuring the in vitro activity of recombinant Synechococcus and Acaryochloris BciA. Genomic comparison reveals that BciB had been replaced by BciA during evolution of the marine cyanobacterium Synechococcus, and coincided with replacement of Fe-superoxide dismutase (SOD) with Ni-SOD. These findings imply that the acquisition of BciA confers an adaptive advantage to cyanobacteria living in low-iron oceanic environments
-
malfunction
loss of 8-vinyl reductase activity in Acaryochloris marina results in the production of 8-vinyl-Chl a and 8-vinyl-Chl d with a negative effect on viability of the cells
malfunction
-
loss of 8-vinyl reductase activity in Acaryochloris marina results in the production of 8-vinyl-Chl a and 8-vinyl-Chl d with a negative effect on viability of the cells
-
metabolism
the enzyme is involved the chlorophyll biosynthetic pathways of oxygenic photosynthetic organisms. At the later steps of chlorophyll biosynthesis, 3,8-divinyl-chlorophyllide (Chlide) a is converted to monovinyl (MV)-Chlide a by DVR. Involvement of DVR in Chl c biosynthesis
metabolism
the majority of (B)Chls utilized for light-harvesting carry an ethyl group at the C8 position (8E) of the macrocycle. This group is produced by the reduction of a vinyl group (8V), catalysed by an 8V reductase, 8VR, resulting in the production of an 8E pigment
metabolism
-
bacteriochlorophyll a (BChl) is an essential pigment for anoxygenic photosynthesis. In late steps of the BChl biosynthesis, the C8 vinyl group and C7=C8 double bond of 8-vinyl chlorophyllide a (8 V-Chlide) are reduced by a C8 vinyl reductase (8VR), BciA (EC 1.3.1.75) or BciB and a nitrogenase-like enzyme, chlorophyllide a oxidoreductase (COR, EC 1.3.7.15), respectively, to produce 3-vinyl-bacteriochlorphyllide a
metabolism
during chlorophyll synthesis, chlorophyllide with a vinyl group at position 8 is produced as a precursor. The divinyl chlorophyllide has two vinyl groups, at positions 3 and 8, respectively. The vinyl group at position 8 is reduced to an ethyl group by 8-vinyl (8V) reductase to form chlorophyllide, which is then esterified with phytyl diphosphate to give chlorophyll. In photosynthetic bacteria, photosynthesis-related genes form clusters. The BciB gene encodes the 8V reductase. BciB contains an [Fe-S] cluster, has FAD as a cofactor, and uses ferredoxin (Fd) as a reductant
metabolism
during chlorophyll synthesis, chlorophyllide with a vinyl group at position 8 is produced as a precursor. The divinyl chlorophyllide has two vinyl groups, at positions 3 and 8, respectively. The vinyl group at position 8 is reduced to an ethyl group by 8-vinyl (8V) reductase to form chlorophyllide, which is then esterified with phytyl diphosphate to give chlorophyll. In photosynthetic bacteria, photosynthesis-related genes form clusters. The BciB gene encodes the 8V reductase. BciB contains an [Fe-S] cluster, has FAD as a cofactor, and uses ferredoxin (Fd) as a reductant. BciB of Synechocystis PCC6803, a model cyanobacterium without chlorophyll b, exhibits both 7-hydroxymethyl chlorophyll a reductase and 8V reductase activity. Synechocystis BciB can convert chlorophyll b to chlorophyll a, but in Synechocystis, such activity has no impact on its metabolism, since it does not synthesize chlorophyll b
metabolism
-
during chlorophyll synthesis, chlorophyllide with a vinyl group at position 8 is produced as a precursor. The divinyl chlorophyllide has two vinyl groups, at positions 3 and 8, respectively. The vinyl group at position 8 is reduced to an ethyl group by 8-vinyl (8V) reductase to form chlorophyllide, which is then esterified with phytyl diphosphate to give chlorophyll. In photosynthetic bacteria, photosynthesis-related genes form clusters. The BciB gene encodes the 8V reductase. BciB contains an [Fe-S] cluster, has FAD as a cofactor, and uses ferredoxin (Fd) as a reductant
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physiological function
functional complementation of an enzyme-deficient DELTAbciB Synechocystis sp. strain PCC 6803
physiological function
-
bacteriochlorophyll a (BChl) is an essential pigment for anoxygenic photosynthesis. In late steps of the BChl biosynthesis, the C8 vinyl group and C7=C8 double bond of 8-vinyl chlorophyllide a (8 V-Chlide) are reduced by a C8 vinyl reductase (8VR), BciA (EC 1.3.1.75) or BciB, and a nitrogenase-like enzyme, chlorophyllide a oxidoreductase (COR), respectively, to produce 3-vinyl-bacteriochlorphyllide a. BciB is a FAD-containing FeS protein that uses reduced ferredoxin as the reductant for the 8-vinyl reduction of 8 V-Chlide or 8 V-PChlide, while BciA utilizes NADPH. BciB is a FAD-containing FeS protein that uses reduced ferredoxin as the reductant for the 8-vinyl reduction of 8 V-Chlide or 8 V-PChlide
physiological function
-
functional complementation of an enzyme-deficient DELTAbciB Synechocystis sp. strain PCC 6803
-
additional information
BciB functions as an 8VR and does not require the presence of an additional subunit
additional information
structural modeling of BciB based on a structure for the FrhB subunit of F420-reducing [NiFe]-hydrogenase of Methanothermobacter marburgensis, overview
additional information
-
structural modeling of BciB based on a structure for the FrhB subunit of F420-reducing [NiFe]-hydrogenase of Methanothermobacter marburgensis, overview
additional information
the enzyme encoded by gene frhB shows 3,8-divinyl protochlorophyllide a 8-vinyl-reductase (ferredoxin) activity and shall be renamed bciB
additional information
-
structural modeling of BciB based on a structure for the FrhB subunit of F420-reducing [NiFe]-hydrogenase of Methanothermobacter marburgensis, overview
-
additional information
-
the enzyme encoded by gene frhB shows 3,8-divinyl protochlorophyllide a 8-vinyl-reductase (ferredoxin) activity and shall be renamed bciB
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expressed in an 8-vinyl chlorophyll a-producing DELTAbciB strain of Synechocystis sp. strain PCC 6803
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expressed in Escherichia coli
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gene AM1_2849, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis, recombinant expression in Escherichia coli
gene bciB or frhB, DNA and amino acid sequence determination and analysis, phylogenetic analysis, frhB is introduced into an 8-vinyl chlorophyll a-producing DELTAbciB strain of Synechocystis sp. strain PCC 6803, and restores synthesis of the pigment with an ethyl group at C-8, demonstrating its activity as 8-vinyl reductase, subcloning in Escherichia coli strain JM109
gene bciB, cloning in Escherichia coli strain JM109, recombinant expression of C-terminally His6-tagged in Escherichia coli strain BL21(DE3). Plasmid pET28-CthaBciB is cotransformed into strain BL21(DE3) along with the plasmid pDB1282, which contains the genes iscS, iscU, iscA, hscA, hscB, and fdx for Fe/S-cluster assembly from Azotobacter vinelandii under the control of an arabinose-inducible promoter to produce Escherichia coli strain AHS-1
gene slr1923, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis, recombinant expression in Escherichia coli
gene slr1923, phylogenetic analysis
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Ito, H.; Tanaka, A.
Evolution of a new chlorophyll metabolic pathway driven by the dynamic changes in enzyme promiscuous activity
Plant Cell Physiol.
55
593-603
2014
Synechocystis sp. (P74473)
brenda
Harada, J.; Mizoguchi, T.; Tsukatani, Y.; Yokono, M.; Tanaka, A.; Tamiaki, H.
Chlorophyllide a oxidoreductase works as one of the divinyl reductases specifically involved in bacteriochlorophyll a biosynthesis
J. Biol. Chem.
289
12716-12726
2014
no activity in Rhodobacter sphaeroides, Rhodopseudomonas palustris, Rhodopseudomonas palustris J1002
brenda
Canniffe, D.P.; Chidgey, J.W.; Hunter, C.N.
Elucidation of the preferred routes of C8-vinyl reduction in chlorophyll and bacteriochlorophyll biosynthesis
Biochem. J.
462
433-440
2014
Synechocystis sp. (P74473)
brenda
Saunders, A.H.; Golbeck, J.H.; Bryant, D.A.
Characterization of BciB: a ferredoxin-dependent 8-vinyl-protochlorophyllide reductase from the green sulfur bacterium Chloroherpeton thalassium
Biochemistry
52
8442-8451
2013
Chloroherpeton thalassium
brenda
Liu, Z.; Bryant, D.A.
Multiple types of 8-vinyl reductases for (bacterio)chlorophyll biosynthesis occur in many green sulfur bacteria
J. Bacteriol.
193
4996-4998
2011
Chlorobium limicola, Chlorobium phaeobacteroides, Pelodictyon clathratiforme, Prosthecochloris aestuarii, Chloroherpeton thalassium, Chlorobium ferrooxidans, Chloroherpeton thalassium ATCC 35110, Pelodictyon clathratiforme DSM 5477, Chlorobium phaeobacteroides DSM 266, Prosthecochloris aestuarii DSM 271, Chlorobium ferrooxidans DSM 13031, Chlorobium limicola DSM 245
brenda
Chen, G.E.; Hitchcock, A.; Jackson, P.J.; Chaudhuri, R.R.; Dickman, M.J.; Hunter, C.N.; Canniffe, D.P.
Two unrelated 8-vinyl reductases ensure production of mature chlorophylls in Acaryochloris marina
J. Bacteriol.
198
1393-1400
2016
Acaryochloris marina
brenda
Canniffe, D.P.; Chidgey, J.W.; Hunter, C.N.
Elucidation of the preferred routes of C8-vinyl reduction in chlorophyll and bacteriochlorophyll biosynthesis
Biochem. J.
462
433-440
2014
Synechocystis sp. PCC 6803 (P74473)
brenda
Saunders, A.H.; Golbeck, J.H.; Bryant, D.A.
Characterization of BciB a ferredoxin-dependent 8-vinyl-protochlorophyllide reductase from the green sulfur bacterium Chloroherpeton thalassium
Biochemistry
52
8442-8451
2013
Chloroherpeton thalassium (B3QYX9), Chloroherpeton thalassium, Chloroherpeton thalassium ATCC 35110 (B3QYX9)
brenda
Chen, G.E.; Hitchcock, A.; Jackson, P.J.; Chaudhuri, R.R.; Dickman, M.J.; Hunter, C.N.; Canniffe, D.P.
Two unrelated 8-vinyl reductases ensure production of mature chlorophylls in Acaryochloris marina
J. Bacteriol.
198
1393-1400
2016
Acaryochloris marina (B0CAB4), Acaryochloris marina MBIC11017 (B0CAB4)
brenda
Ito, H.; Tanaka, A.
Evolution of a new chlorophyll metabolic pathway driven by the dynamic changes in enzyme promiscuous activity
Plant Cell Physiol.
55
593-603
2014
Synechocystis sp. PCC 6803 (P74473)
brenda
Suehiro, H.; Tanaka, R.; Ito, H.
Distribution and functional analysis of the two types of 8-vinyl reductase involved in chlorophyll biosynthesis in marine cyanobacteria
Arch. Microbiol.
203
3565-3575
2021
Acaryochloris marina (B0CAB4), Synechocystis sp. PCC 6803 (P74473), Acaryochloris marina MBIC11017 (B0CAB4)
brenda
Yamamoto, H.; Mizoguchi, T.; Tsukatani, Y.; Tamiaki, H.; Kurisu, G.; Fujita, Y.
Chlorophyllide a oxidoreductase preferentially catalyzes 8-vinyl reduction over B-ring reduction of 8-vinyl chlorophyllide a in the late steps of bacteriochlorophyll biosynthesis
ChemBioChem
21
1760-1766
2020
Chloroherpeton thalassium
brenda