In a new study published in Biochemical Journal, researchers have discovered with potential human health impacts in a parchment tubeworm, the marine invertebrate Chaetopterus sp., and found that the tubeworm have a ferritin with the fastest catalytic performance ever described, nearly eight times faster than that of human capabilities.

Ferritin is an important protein found in nearly all living organisms as it manages iron metabolism in cells by storing and releasing it in a controlled manner. In humans, it is critical to iron storage and iron metabolism, helping balance iron in the blood. The discovery has important human health implications for biomedical research, as ferritin is an essential protein for those with iron deficiency and overall iron metabolism issues.

The discovery can be a new tool in future research of ferritin to use in patients, thanks to its biocompatibility and ability to carry, protect and deliver small molecules as medication to specific targets. The parchment tubeworm has bioluminescent capabilities. The species also has the unique ability to keep its blue light glowing for hours, and sometimes days on end, significantly longer than most bioluminescent organisms that typically illuminate only for milliseconds or seconds.

A study published in 2016 in Scientific Reports suggested that ferritin in the worm's mucus enabled the sustained light production. Because of the light-stimulating effect, the presence of ferritin in the mucus was considered of interest by the researchers to further understand its role in this unusual light-production pattern in the tubeworm. The link to bioluminescence is incredibly important, and the team wanted to understand how ferritin influences bioluminescence and why ferritin works so much faster in this organism.

They described ferritin as being shaped like a soccer ball, with openings that take up iron when available, store it and release it when needed. It could help target medication release, function as a safe contrast agent, while also being used for water treatment by selectively taking up and storing contaminants. The researchers tested two different approaches to measure enzyme response, covering different time scales. Both approaches compared the reactions of worm ferritin with human ferritin.

In the first approach, iron was added to reaction tubes containing the respective ferritins, after which the remaining amount of ferrous iron left in solution was measured over time (1-2 hours). The second analyzed on millisecond scale how much iron oxide was created inside the ferritin, indicated by the generation of "rust" coloration the tube. Both approaches determined the worm ferritin converted iron significantly faster.

Dimitri Deheyn the lead investigator of the study said, "We were surprised to discover that even though the tubeworm ferritin is very similar to human ferritin, it outperforms the human variant, by a lot. There are major biotechnological research implications to this finding, in particular for the many labs that develop ferritin applications."