The process of bioluminescence requires the presence of two chemicals, a pigment called luciferin and an enzyme called luciferase. When luciferin reacts with oxygen in the presence of the catalyst luciferase, a by product known as oxyluciferin is produced. This oxyluciferin is the luminescent light which is emitted by bioluminescent creatures.
However, it has been recently identified that some bioluminescence processes do not involve the enzyme luciferase. These reactions occur by combining a chemical called photo protein with the help of an ion of calcium to produce light.
The pigment luciferin is self synthesized in certain organisms; although other organisms may absorb it by consumption of food or by sharing a symbiotic relationship with another organisms. The color that is generated in bioluminescent organisms results from the arrangement of molecules of luciferin.""
Is Bioluminescence Mechanism the Same as Chemiluminescence? Keto-Oxyluciferin Can Emit Red light in Solution and Yellow-Green light in Luciferase. Artificial Color Tuning of Firefly Luminescence: Theoretical Mutation by Tuning Electrostatic Interactions between Protein and Luciferin www.fukui.kyoto-u.ac.jp/users/hasegawa/hase_files/FireflyLuciferin.html
Notice the points: luciferase from sea pansy. Biological Sources of Luciferase Sea_pansy_creditedAlthough luciferase isolated from the firefly beetle (Photinus pyralis) is the most frequently used bioluminescent reporter, other luciferases have been identified in various species with differing kinetics, substrate requirements and photon emission wavelengths. Renilla luciferase from the sea pansy (Renilla reniformis) emits a blue light with a peak emission at 480nm upon catalyzing a chemical reaction with the substrate coelenterazine and is likely the second most commonly used luciferase. Other organisms from which luciferases have been cloned from include click beetles (Pyrophorus plagiophthalmus), railroad worm (Phrixothrix hirtus), and a variety of marine crustaceans. Many of these luciferases have been subjected to further engineering to improve upon the properties of the native enzyme, which are summarized in Table 2 below.
...... photo protein with the help of an ion of calcium to produce light.".....
Photo proteins: Chemical Effects on Light Emission by Photoproteins Shannon McVay, Mississippi University for Women Mentor: Dr. Steven Hadock Summer 2002 Keywords: calcium-activated photoproteins, pH level variation, Mitrocoma cellularia
ABSTRACT Several experiments in the past have been successfully conducted where a shift in the spectra of some bioluminescent organisms occurred by the use of pH level variations. The following experiment attempted to replicate the same results by varying the pH levels on extracts of the ctenophore, Mitrocoma cellularia and the siphonophore,Chuniphyes multidentata . The experiment was originally intended to focus on bioluminescent organism that were known to produce dual wavelengths, but due to a lack of dual wavelength producing organisms available to the experimenters, Mitrocoma cellularia was more abundant and was therefore used. It’s extract ended up having a spectra shift from 465 nm(blue region) to 490nm(blue-green region) at pH levels 8 and 9, respectively. Whereas the dual wave length producing siphonophore available, Chuniphyes multidentata’s extract did not have a spectra l shift caused by pH level variation. However, the spectral shift that occurred in the Mitrocoma extract gives hope that such a shift is possible in other bioluminescent gelatinous creatures, including dual wavelength producers.
It is the photoprotein that is similar or is a fluorophore.
......However, it has been recently identified that some bioluminescence processes do not involve the enzyme luciferase. These reactions occur by combining a chemical called photo protein with the help of an ion of calcium to produce light."........
if we would get the spectra for the bioilluminent freq(photoproteins) we could find the source of the product? these photo proteins would be Light frequency. They would have a wave length, that could be measured.
Then if we could find the acoutics (RF) of clicking in ears we could find the source protein?
If we could find the movement (magnetesomes or magnetic particles) we could measure (EMF)and locate source.
If we could prove the quantum dots at ends of filaments, we could prove source of energy as in (ELF
(MW) measurements could locate the source of MW or release of these waves.
So, if Photoproteins, RF, EMF, ELF, QD and MW can all be measured, then lets go for it.
Moreover, the success of optogenetics has inspired discussions of other possible classes of control (e.g., magnetogenetics, acoustogenetics) in which other modalities of energy delivery would be captured by distinct classes of engineered, targetable-molecular-energy antenna-like elements expressed in specific classes of cells. ...
tash: Hi skizit, I have watched all your videos on youtube and cant thank you enough for all you have educated me on. I cry for you alot and a bit for me. I was wanting to send you photos of what is raining down everyday here in Australia in hope you can tell me
Dec 11, 2019 23:28:22 GMT -5
tash: not sure where to send them as hush mail and rocket mail bounced back
Dec 11, 2019 23:30:03 GMT -5