Bacteriochlorophylls a
* Please be kindly noted products are not for therapeutic use. We do not sell to patients.
| Category | Others |
| Catalog number | BBF-00255 |
| CAS | 17499-98-8 |
| Molecular Weight | 911.50 |
| Molecular Formula | C55H74MgN4O6 |
| Purity | ≥95% |
Online Inquiry
Description
Bacteriochlorophylls a is produced by the strain of Chlorobiea and Rhodospirillinea. It has a structural skeleton similar to chlorophyll of higher plants.
Specification
| Synonyms | Bacteriochlorophyll; C11242 |
| Storage | -20ºC |
| IUPAC Name | magnesium;methyl (3R,11R,12R,21S,22S)-16-acetyl-11-ethyl-12,17,21,26-tetramethyl-4-oxo-22-[3-oxo-3-[(E,7R,11R)-3,7,11,15-tetramethylhexadec-2-enoxy]propyl]-23,25-diaza-7,24-diazanidahexacyclo[18.2.1.15,8.110,13.115,18.02,6]hexacosa-1(23),2(6),5(26),8,10(25),13,15,17,19-nonaene-3-carboxylate |
| Canonical SMILES | CCC1C(C2=CC3=C(C(=C([N-]3)C=C4C(C(C(=N4)C5=C6C(=C(C(=CC1=N2)[N-]6)C)C(=O)C5C(=O)OC)CCC(=O)OCC=C(C)CCCC(C)CCCC(C)CCCC(C)C)C)C)C(=O)C)C.[Mg+2] |
| InChI | InChI=1S/C55H75N4O6.Mg/c1-13-39-34(7)41-29-46-48(38(11)60)36(9)43(57-46)27-42-35(8)40(52(58-42)50-51(55(63)64-12)54(62)49-37(10)44(59-53(49)50)28-45(39)56-41)23-24-47(61)65-26-25-33(6)22-16-21-32(5)20-15-19-31(4)18-14-17-30(2)3;/h25,27-32,34-35,39-40,51H,13-24,26H2,1-12H3,(H-,56,57,58,59,60,62);/q-1;+2/p-1/b33-25+;/t31-,32-,34-,35+,39-,40+,51-;/m1./s1 |
| InChI Key | DSJXIQQMORJERS-AGGZHOMASA-M |
Properties
| Appearance | Light Green to Blue-Green Powder |
| Boiling Point | 877.3ºC at 760mmHg |
Reference Reading
1.Origin of Bacteriochlorophyll a and the Early Diversification of Photosynthesis.
Cardona T1. PLoS One. 2016 Mar 8;11(3):e0151250. doi: 10.1371/journal.pone.0151250. eCollection 2016.
Photosynthesis originated in the domain Bacteria billions of years ago; however, the identity of the last common ancestor to all phototrophic bacteria remains undetermined and speculative. Here I present the evolution of BchF or 3-vinyl-bacteriochlorophyll hydratase, an enzyme exclusively found in bacteria capable of synthetizing bacteriochlorophyll a. I show that BchF exists in two forms originating from an early divergence, one found in the phylum Chlorobi, including its paralogue BchV, and a second form that was ancestral to the enzyme found in the remaining anoxygenic phototrophic bacteria. The phylogeny of BchF is consistent with bacteriochlorophyll a evolving in an ancestral phototrophic bacterium that lived before the radiation event that gave rise to the phylum Chloroflexi, Chlorobi, Acidobacteria, Proteobacteria, and Gemmatimonadetes, but only after the divergence of Type I and Type II reaction centers. Consequently, it is suggested that the lack of phototrophy in many groups of extant bacteria is a derived trait.
2.Perturbation Of Bacteriochlorophyll Molecules In Fenna-Matthews-Olson Protein Complexes Through Mutagenesis Of Cysteine Residues.
Saer R1, Orf GS2, Lu X3, Zhang H4, Cuneo MJ3, Myles DA3, Blankenship RE5. Biochim Biophys Acta. 2016 Apr 22. pii: S0005-2728(16)30103-7. doi: 10.1016/j.bbabio.2016.04.007. [Epub ahead of print]
The Fenna-Matthews-Olson (FMO) pigment-protein complex in green sulfur bacteria transfers excitation energy from the chlorosome antenna complex to the reaction center. In understanding energy transfer in the FMO protein, the individual contributions of the bacteriochlorophyll pigments to the FMO complex's absorption spectrum could provide detailed information with which molecular and energetic models can be constructed. The absorption properties of the pigments, however, are such that their spectra overlap significantly. To overcome this, we used site-directed mutagenesis to construct a series of mutant FMO complexes in the model green sulfur bacterium Chlorobaculum tepidum (formerly Chlorobium tepidum). Two cysteines at positions 49 and 353 in the C. tepidum FMO complex, which reside near hydrogen bonds between BChls 2 and 3, and their amino acid binding partners serine 73 and tyrosine 15, respectively, were changed to alanine residues.
3.The photoheterotrophic growth of bacteriochlorophyll synthase-deficient mutant of Rhodobacter sphaeroides is restored by I44F mutant chlorophyll synthase of Synechocystis sp. PCC 6803.
Kim EJ1, Kim H1, Lee JK1. J Microbiol Biotechnol. 2016 Feb 12. doi: 10.4014/jmb.1601.01019. [Epub ahead of print]
Chlorophyll synthase (ChlG) and bacteriochlorophyll synthase (BchG) have a high degree of substrate specificity. The BchG mutant of Rhodobacter sphaeroides, BG1 strain, is photosynthetically incompetent. When BG1 harboring chlG of Synechocystis sp. PCC 6803 was cultured photoheterotrophically, colonies arose at a frequency of approximately 10-8. All the suppressor mutants were determined to have the same mutational change ChlGI44F. The mutated enzyme ChlGI44F showed BchG activity. Remarkably, BchGF28I, which has the substitution of F at the corresponding 28th residue to I, showed ChlG activity. The Km values of ChlGI44F and BchGF28I for their original substrates, chlorophyllide (Chlide) a and bacteriochlorophyllide (Bchlide) a, respectively, were not affected by the mutations, but the Km values of ChlGI44F and BchGF28I for the new substrates Bchlide a and Chlide a, respectively, were more than ten-fold larger than those for their original substrates, suggesting the lower affinities for new substrates.
Recommended Products
| BBF-05730 | Abamectin | Inquiry |
| BBF-04659 | Spinosyn J | Inquiry |
| BBF-03800 | Moxidectin | Inquiry |
| BBF-05727 | Tacrolimus monohydrate | Inquiry |
| BBF-03791 | Daptomycin | Inquiry |
| BBF-03819 | Spinosyn A | Inquiry |
Bio Calculators
* Our calculator is based on the following equation:
Concentration (start) x Volume (start) = Concentration (final) x Volume (final)
It is commonly abbreviated as: C1V1 = C2V2
* Total Molecular Weight:
g/mol
Tip: Chemical formula is case sensitive. C22H30N4O √ c22h30n40 ╳
