The researchers patented the use
of ferredoxins and FNR to target the enzymes needed to make light - activated molecules.
So an enzyme
called Ferredoxin - NADP reductase, or FNR, played the role of outlet adapter.
Super-complexes, able to specifically perform linear or cyclic photosynthetic electron flow have been identified, and all contain the
enzyme ferredoxin NADP + reductase (FNR), which is also present as a soluble protein.
It demonstrates that in the photosynthetic alga Chlamydomonas, the
protein ferredoxin - 5 is critical for growth in dark and for proper membrane organization.
Ferredoxin exists under a different form in animal cells, which isn't compatible with its plant and bacteria cousin.
For the power cord, they used bacterial and
plant ferredoxin, an iron and sulfur protein that brings about electron transfer in a number of reactions.
Photosynthetic organisms typically have multiple different types
of ferredoxins, although little is known about how their functions differ.
Team members Julie Nixon and John Samuelson of Harvard University found the 35 - base intron in the middle of the gene for a protein
called ferredoxin.
Just for my curiosity, who doubts the conclusion of the experiment, i.e. that
mitochondrial ferredoxin is required for assembly of cytosolic iron sulfur proteins?
Chlamydomonas has several
ferredoxins, including the ferredoxin - 5 protein described in this study.
(In the light, however, another member of
the ferredoxin family may take on this responsibility, which is why the aberrant membrane structure is only observed in plants that are maintained in darkness.).
The work presented suggests that
the ferredoxin variants, including ferredoxin - 5, may each have specialized metabolic roles in the cell.
This result indicates that when the alga is in the dark,
ferredoxin - 5 specifically donates electrons to enzymes that specialize in desaturating fatty acids; it may also donate electrons to other processes in the dark.
Ferredoxin - 5 is a member of a family of small iron - sulfur proteins that provide the electrons needed to drive various metabolic reactions in the cell.
The team found that a specific mutant lacking
the ferredoxin - 5 protein was unable to grow in the dark (in the nighttime) or perform normal metabolic functions, but it had no trouble growing during the light (in the daytime).
«This work homed in on the role of
ferredoxin - 5 and factors critical for photosynthetic organisms to switch between daytime and nighttime metabolism,» Grossman said.
The ferredoxin - 5 mutant shows marked alterations in the bond structure of many of these fatty acids, which changes the degree of saturation in the fatty acids present in the membranes.
The team's findings suggest that one of the biochemical reactions that
ferredoxin - 5 drives through its electron - donating abilities is this alteration in the saturation state of fatty acids.
Ferredoxin, the electron carrier, hands over its charge to TPN.