The enzyme catalyses the successive reduction of the geranylgeraniol esterifying group to phytol, reducing three out of four double bonds, and transforming geranylgeranyl bacteriochlorophyllide a via dihydrogeranylgeranyl bacteriochlorophyllide a and tetrahydrogeranylgeranyl bacteriochlorophyllide a to bacteriochlorophyll a. The enzyme can also accept the pheophytin derivative geranylgeranyl bacteriopheophytin, converting it to bacteriopheophytin a.
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The enzyme catalyses the successive reduction of the geranylgeraniol esterifying group to phytol, reducing three out of four double bonds, and transforming geranylgeranyl bacteriochlorophyllide a via dihydrogeranylgeranyl bacteriochlorophyllide a and tetrahydrogeranylgeranyl bacteriochlorophyllide a to bacteriochlorophyll a. The enzyme can also accept the pheophytin derivative geranylgeranyl bacteriopheophytin, converting it to bacteriopheophytin a.
a mutant in orf391 synthesizes bacteriochlorophyll a that is esterified with geranylgeraniol rather than the normal phytol. Strains that accumulate geranylgeraniol-esterified bacteriochlorophyll a exhibit reduced photosynthetic growth capability compared to that observed with the parent strain which synthesizes bacteriochlorophyll a that is esterified with phytol. But synthesis of geranylgeranyl bacteriochlorophyllide a does not per se impair function of the reaction center complex nor energy transfer from the light harvesting complex
a transposon mutant of gene bchP encoding geranylgeranyl-bacteriochlorophyll reductase possesses a structurally modified photosystem assembled with bacteriochlorophyll esterified with geranylgeraniol, rather than with phytol
the bchP mutant T6G5 of purple photosynthetic bacterium Rhodobacter sphaeroides is blocked in the terminal hydrogenation steps of bacteriochlorophyll a biosynthesis. The mutant possesses only bacteriochlorophyll esterified with geranylgeraniol and has a reduced cellular level of the light-harvesting LH2 complex
the CT2256-deleted mutant shows accumulation of chlorophyllous pigments esterified with the geranylgeranyl group and photosynthetic competence, phenotype, overview
the enzyme only catalyzes the reduction of the isoprenoid moiety of bacteriopheophytin. It might be a naturally occurring bchP mutant with an insertion mutation that may have been the initial cause of a partial loss of function
the CT2256-deleted mutant shows accumulation of chlorophyllous pigments esterified with the geranylgeranyl group and photosynthetic competence, phenotype, overview
the bchP mutant T6G5 of purple photosynthetic bacterium Rhodobacter sphaeroides is blocked in the terminal hydrogenation steps of bacteriochlorophyll a biosynthesis. The mutant possesses only bacteriochlorophyll esterified with geranylgeraniol and has a reduced cellular level of the light-harvesting LH2 complex
a mutant in orf391 synthesizes bacteriochlorophyll a that is esterified with geranylgeraniol rather than the normal phytol. Strains that accumulate geranylgeraniol-esterified bacteriochlorophyll a exhibit reduced photosynthetic growth capability compared to that observed with the parent strain which synthesizes bacteriochlorophyll a that is esterified with phytol. But synthesis of geranylgeranyl bacteriochlorophyllide a does not per se impair function of the reaction center complex nor energy transfer from the light harvesting complex
esterification of bacteriochlorophyllide a initially involves the addition of a geranylgeraniol group followed by sequential reduction of the geranylgeraniol moiety tophytol which is the end product of the pathway. Synthesis of geranylgeraniol-esterified bacteriochlorophyll does not affect the energy transfer rate from light harvesting to reaction center complexes nor the electron transfer function as measured by the yield of electron transfer to the primary and secondary quinones, the charge recombination rate from the quinones, and the rate of cytochrome c2 oxidation. Pathway for synthesis of bacteriochlorophyll from bacteriochlorophyllide, overview
requirement of Rhodospirillum rubrum for phytylated bacteriopheophytin, a potential link between the absence of light-harvesting complex 2 and of phytylated bacteriochlorophyll from the wild-type bacterium. In addition to bacteriochlorophyll, the reaction center of purple bacteria contains two bacteriopheophytin molecules, one of which is the first clearly resolved acceptor of electrons, following electron transfer from the bacteriochlorophyll dimer. Proposed pathway for reduction of geranylgeranyl bacteriopheophytin a in Rhodospirillum rubrum, reduction proceeds via dihydro-GG-esterified and tetrahydro-GG-esterified intermediates to the final product, phytylated bacteriopheophytin
the enzyme catalyzes the stepwise hydrogenation of geranylgeraniol to phytol during bacteriochlorophyll a biosynthesis, pathway for the phytylation of bacteriochlorophyll a, overview
esterification of bacteriochlorophyllide a initially involves the addition of a geranylgeraniol group followed by sequential reduction of the geranylgeraniol moiety tophytol which is the end product of the pathway. Synthesis of geranylgeraniol-esterified bacteriochlorophyll does not affect the energy transfer rate from light harvesting to reaction center complexes nor the electron transfer function as measured by the yield of electron transfer to the primary and secondary quinones, the charge recombination rate from the quinones, and the rate of cytochrome c2 oxidation. Pathway for synthesis of bacteriochlorophyll from bacteriochlorophyllide, overview
the bacteriochlorophyll of the purple photosynthetic bacterium Rhodobacter sphaeroides is esterified with phytol. The presence of this alcohol moiety is essential for the correct assembly of the photosynthetic apparatus. The enzyme is essential and responsible for the reduction of the alcohol moiety of (bacterio)chlorophyll to phytol
the enzyme is involved esterification of bacteriochlorophyll a with DELTA2,6-phytadienol and phytol, respectively, which is produced by reduction of the geranylgeranyl group at the C-17 propionate residue
the enzyme is responsible for the reduction of the isoprenoid moiety of bacteriochlorophyll (Bchl) from geranylgeraniol (GG) to phytol, it also catalyzes the reduction of the isoprenoid moiety of bacteriopheophytin
the enzyme is involved esterification of bacteriochlorophyll a with DELTA2,6-phytadienol and phytol, respectively, which is produced by reduction of the geranylgeranyl group at the C-17 propionate residue
a transposon mutant of gene bchP encoding geranylgeranyl-bacteriochlorophyll reductase possesses a structurally modified photosystem assembled with bacteriochlorophyll esterified with geranylgeraniol, rather than with phytol
a transposon mutant of gene bchP encoding geranylgeranyl-bacteriochlorophyll reductase possesses a structurally modified photosystem assembled with bacteriochlorophyll esterified with geranylgeraniol, rather than with phytol
construction of a a hybrid gene consisting of the 5'half of Rhodospirillum rubrum bchP and the 3' half of Rhodobacter sphaeroides bchP, with the fragments fused as for bchPDELTAx, possesses neither geranylgeranyl-bacteriopheophytin reductase nor geranylgeranyl-bacteriochlorophyll a reductase activity. When complenmentation of the mutant is attempted with a similar fusion between the 5' half of Rhodobacter sphaeroides bchP and the 3' half of Rhodospirillum rubrum bchP, expressed in plasmid pSK1bchPS/PR, not only is BpheaP biosynthesis restored, but approximately 10% of the Bchl present is found to be esterified with dihydro-GG. Complete restoration of both BchlaP and BpheaP synthesis is achieved by using the positive control plasmid, pSK1bchPS/PS, in which the two relevant Rhodobacter sphaeroides bchP fragments are reunited
construction of a a hybrid gene consisting of the 5'half of Rhodospirillum rubrum bchP and the 3' half of Rhodobacter sphaeroides bchP, with the fragments fused as for bchPDELTAx, possesses neither geranylgeranyl-bacteriopheophytin reductase nor geranylgeranyl-bacteriochlorophyll a reductase activity. When complenmentation of the mutant is attempted with a similar fusion between the 5' half of Rhodobacter sphaeroides bchP and the 3' half of Rhodospirillum rubrum bchP, expressed in plasmid pSK1bchPS/PR, not only is BpheaP biosynthesis restored, but approximately 10% of the Bchl present is found to be esterified with dihydro-GG. Complete restoration of both BchlaP and BpheaP synthesis is achieved by using the positive control plasmid, pSK1bchPS/PS, in which the two relevant Rhodobacter sphaeroides bchP fragments are reunited
the bchP mutant T6G5 of purple photosynthetic bacterium Rhodobacter sphaeroides is blocked in the terminal hydrogenation steps of bacteriochlorophyll a biosynthesis. The mutant possesses only bacteriochlorophyll esterified with geranylgeraniol and has a reduced cellular level of the light-harvesting LH2 complex. Upon heterologous expression of the Synechocystis bchP homologue encoded by gene chlP, not only are hydrogenated forms of geranylgeranyl bacteriochlorophyllide a (bchlaGG) detectable, but the level of LH2 is increased, phenotype, overview
the bchP mutant T6G5 of purple photosynthetic bacterium Rhodobacter sphaeroides is blocked in the terminal hydrogenation steps of bacteriochlorophyll a biosynthesis. The mutant possesses only bacteriochlorophyll esterified with geranylgeraniol and has a reduced cellular level of the light-harvesting LH2 complex. Upon heterologous expression of the Synechocystis bchP homologue encoded by gene chlP, not only are hydrogenated forms of geranylgeranyl bacteriochlorophyllide a (bchlaGG) detectable, but the level of LH2 is increased, phenotype, overview
generation of a gene CT2256 deletion mutant, which almost shows no apparent phenotype compared to the wild-type. The purple bacterium Rhodobacter capsulatus mutant strain DB391 defective in the bchP gene is partially complemented with the CT2256 gene, bacteriochlorophyllide a is synthesized in the mutant in addition to accumulating other intermediates, phenotype, overview
generation of a gene CT2256 deletion mutant, which almost shows no apparent phenotype compared to the wild-type. The purple bacterium Rhodobacter capsulatus mutant strain DB391 defective in the bchP gene is partially complemented with the CT2256 gene, bacteriochlorophyllide a is synthesized in the mutant in addition to accumulating other intermediates, phenotype, overview
construction of a hybrid gene consisting of the 5' half of Rhodospirillum rubrum bchP and the 3' half of Rhodobacter sphaeroides bchP, with the fragments fused as for bchPDELTAx, possesses neither geranylgeranyl-bacteriopheophytin reductase nor geranylgeranyl-bacteriochlorophyll a reductase activity. When complenmentation of the mutant is attempted with a similar fusion between the 5' half of Rhodobacter sphaeroides bchP and the 3' half of Rhodospirillum rubrum bchP, expressed in plasmid pSK1bchPS/PR, not only is BpheaP biosynthesis restored, but approximately 10% of the Bchl present is found to be esterified with dihydro-GG. Complete restoration of both BchlaP and BpheaP synthesis is achieved by using the positive control plasmid, pSK1bchPS/PS, in which the two relevant Rhodobacter sphaeroides bchP fragments are reunited
construction of a hybrid gene consisting of the 5' half of Rhodospirillum rubrum bchP and the 3' half of Rhodobacter sphaeroides bchP, with the fragments fused as for bchPDELTAx, possesses neither geranylgeranyl-bacteriopheophytin reductase nor geranylgeranyl-bacteriochlorophyll a reductase activity. When complenmentation of the mutant is attempted with a similar fusion between the 5' half of Rhodobacter sphaeroides bchP and the 3' half of Rhodospirillum rubrum bchP, expressed in plasmid pSK1bchPS/PR, not only is BpheaP biosynthesis restored, but approximately 10% of the Bchl present is found to be esterified with dihydro-GG. Complete restoration of both BchlaP and BpheaP synthesis is achieved by using the positive control plasmid, pSK1bchPS/PS, in which the two relevant Rhodobacter sphaeroides bchP fragments are reunited
gene bchP, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)pLysS. The recombinant enzyme complements the bchP insertion mutant T6G5
gene chfP, DNA and amino acid sequence determination and analysis, the enzyme partially complements a bchP mutant T6G5 of purple photosynthetic bacterium Rhodobacter sphaeroides, which is blocked in the terminal hydrogenation steps of bacteriochlorophyll a biosynthesis. The mutant possesses only bacteriochlorophyll esterified with geranylgeraniol and has a reduced cellular level of the light-harvesting LH2 complex. Upon heterologous expression of the Synechocystis bchP homologue, not only are hydrogenated forms of geranylgeranyl bacteriochlorophyllide a (bchlaGG) detectable, but the level of LH2 is increased, sequence comparison with gene chP from Rhodobacter sphaeroides strain NCIB 8253
Molecular genetic analysis of terminal steps in bacteriochlorophyll a biosynthesis: characterization of a Rhodobacter capsulatus strain that synthesizes geranylgeraniol-esterified bacteriochlorophyll a
Accumulation of chlorophyllous pigments esterified with the geranylgeranyl group and photosynthetic competence in the CT2256-deleted mutant of the green sulfur bacterium Chlorobium tepidum