The idea is not as odd as it may sound; scientists studying other environments have previously observed
nitrite oxidoreductase working in reverse when microbial growth is inhibited.
Glutaredoxins (GRXs) are
ubiquitous oxidoreductases implicated in redox homeostasis that catalyze the reversible reduction of disulfide bonds.
Hence, we linked output of our complete synthetic sensing gene circuit to the de-greening gene circuit by placing its genes (diRNA POR,
protochlorophyllide oxidoreductase; AtChlase, chlorophyllase; AtRCCR, red chlorophyll catabolite reductase)[7] under control of the PlantPho promoter (Figure 1).
It also illustrates a strategy for mechanistic study that can be applied to
other oxidoreductase enzymes and to biomimetic complexes.
Functional studies remain necessary to validate these hypothetical pathways, and to determine the specific pathway of ammonia conversion in the absence of a defined homologue for
hydroxylamine oxidoreductase.
Additionally, the purple sweet potatoes increased levels of antioxidants significantly including
quinine oxidoreductase - 1, heme oxygenase - 1, and GSTα.
Sunlight has been found to inhibit nitrite oxidation, and the enzyme microbes normally use to convert nitrite to nitrate, called
nitrite oxidoreductase, can begin to work in reverse, converting nitrate to nitrite.
These antioxidants include glutathione and ascorbic acid and are substrates for enzymes such as peroxidases and
oxidoreductases.
The assembly includes the cytoplasmic (T1) domain of the integral membrane α subunit together with
the oxidoreductase β subunit in a fourfold symmetric T14β4 complex.