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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

?
-
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
?
-
-
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
?
-
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
-
-
?
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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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.
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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
-
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
-
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.