Queen pricks her finger whilst tatting!

…and that, according to the fable, is how the exquisite lace doily of Daucus carota got a single dark red (or blue) floret as the centerpiece of its umbelliferous inflorescence.

The queen was Anne of Denmark, of course (See biography) and the plant is the Wild Carrot, the same species (but different sub-species) as our orange root veggie.

I have spent several hours in the past couple of weeks photographing this amazing plant in various stages of demonstrating its tatting talent. So some separate posts will certainly be required to do justice to the development of the blooms. But this time I want us to think together about that tiny central blossom.

How does this plant “know” how to make one pigmented floret in the exact center of a sea of white? And how does it know how to synthesize those complex anthocyanin molecules and pour them into the central vacuoles of the cells of that one floret? It’s genetically programmed, of course. But saying that is letting us off far too easy. The following description of the biosynthesis of anthocyanins should convince us of the complexity of the process:

Anthocyanin pigments are assembled like all other

flavonoids from two different streams of chemical raw materials in the cell:
One stream involves the shikimate pathway to produce the amino acid phenylalanine. (see phenylpropanoids)
The other stream produces 3 molecules of malonyl-CoA, a C3 unit from a C2 unit (acetyl-CoA). These streams meet and are coupled together by the enzyme chalcone synthase (CHS), which forms an intermediate chalcone via a polyketide folding mechanism that is commonly found in plants.
The chalcone is subsequently isomerized by the enzyme chalcone isomerase (CHI) to the prototype pigment naringenin.
Naringenin is subsequently oxidized by enzymes such as flavanone hydroxylase (FHT or F3H), flavonoid 3' hydroxylase and flavonoid 3' 5'-hydroxylase.
These oxidation products are further reduced by the enzyme dihydroflavonol 4-reductase (DFR) to the corresponding leucoanthocyanidins.
It was believed that leucoanthocyanidins are the immediate precursors of the next enzyme, a dioxygenase referred to as anthocyanidin synthase (ANS) or leucoanthocyanidin dioxygenase (LDOX). It was recently shown however that flavan-3-ols, the products of leucoanthocyanidin reductase (LAR), are the true substrates of ANS/LDOX.
The resulting, unstable anthocyanidins are further coupled to sugar molecules by enzymes like UDP-3-O-glucosyl transferase to yield the final relatively stable anthocyanins.

More than five enzymes* are thus required to synthesize these pigments, each working in concert. Any even minor disruption in any of the mechanisms of these enzymes by either genetic or environmental factors would halt anthocyanin production. (Source)

*Enzymes, large, three-dimensional protein molecules, are far more complex than the anthocyanins they are responsible for synthesizing.

We all understood that, right? Just think how long it took very smart biochemists, working in million-dollar, government-funded laboratories, to work out those biochemical pathways! And we are expected to believe that “nature,” given millions of years, figured out how to do it by a long series of DNA-damaging accidents and natural selection!

Right—and we are all just “lucky mud.” Probability theorists would tell us that the "Queen Anne's lace-making boo-boo tale" would be infinitely more likely than any evolutionary just-so story in explaining the existence of the magical Daucus carota "blood spot"-- or even one of the machine-like enzymes necessary to make it!

(Note: click on the photos to magnify the magnificence of the Queen's work.)

Soli Deo Gloria!