# Unexpected Dual Function of Plant YUCCA Enzymes Links Chlorophyll Catabolism to Auxin Homeostasis

**Authors:** Sina Rütschlin, Lei Zhang, Cornelia A. Karg, Michael Zwerger, Johanna M. Gostner, Simone Moser, Robin Teufel

PMC · DOI: 10.1002/anie.202525568 · Angewandte Chemie (International Ed. in English) · 2026-01-21

## TL;DR

This study reveals that some YUCCA enzymes in plants not only help make auxin but also break down chlorophyll, linking these processes to plant aging.

## Contribution

The discovery of a dual enzymatic function in YUCCA10 enzymes, connecting chlorophyll catabolism to auxin biosynthesis.

## Key findings

- YUCCA10 enzymes from Vitis vinifera and Coffea arabica catalyze chlorophyll catabolite formation via Baeyer–Villiger oxidation and γ-lactam-forming deformylation.
- Chlorophyll catabolites inhibit YUCCA10-mediated auxin biosynthesis in vitro, suggesting feedback regulation during senescence.
- Arabidopsis thaliana YUCCA10 lacks chlorophyll catabolism activity but retains auxin biosynthesis function.

## Abstract

Chlorophyll (Chl) metabolism is pivotal to both photosynthesis and plant senescence and represents one of the most fundamental biological processes on Earth with an estimated annual turnover of 1 billion tons. During Chl degradation, only early catabolites and corresponding enzymes are well characterized, whereas for late‐stage degradation products it remains often unclear if their formation involves specific enzymes. Here, we report that the ubiquitous YUCCA10 enzymes from the YUCCA flavin‐containing monooxygenase (FMOs) family in land plants, normally implicated in the biosynthesis of indole‐3‐acetic acid (IAA) as the primary form of auxin, surprisingly catalyze the production of several predominant Chl catabolites via mechanistically distinct Baeyer–Villiger oxidation and subsequent hydrolytic γ‐lactam‐forming deformylation reactions. These historically postulated but hitherto undiscovered Chl degradation steps on several high molecular weight chl catabolites were verified for YUCCA10 from Vitis vinifera and Coffea arabica, while YUCCA10 from Arabidopsis thaliana lacked this activity. In contrast, all three homologs were able to catalyze the rate‐limiting key step in IAA biosynthesis, akin to other YUCCA enzymes. Interestingly, Chl catabolites at physiological concentrations impaired IAA formation by YUCCA10 in vitro, suggesting a key role in leaf senescence through enzymatic feedback regulation of auxin levels.

YUCCA enzymes are well known to catalyze the main step of auxin biosynthesis in plants. Here, a hitherto undescribed dual function was discovered, revealing that some YUCCAs also act in chlorophyll degradation. In vitro feedback regulation furthermore suggests a link between chlorophyll degradation and hormone homeostasis and a physiological role of accumulating chlorophyll catabolites for plant senescence.

## Linked entities

- **Genes:** YUC10 (Flavin-containing monooxygenase family protein) [NCBI Gene 841313]
- **Proteins:** YUC10 (Flavin-containing monooxygenase family protein)
- **Chemicals:** chlorophyll (PubChem CID 156620228), indole-3-acetic acid (PubChem CID 802), IAA (PubChem CID 802)
- **Species:** Vitis vinifera (taxon 29760), Coffea arabica (taxon 13443), Arabidopsis thaliana (taxon 3702)

## Full-text entities

- **Genes:** YUC10 (Flavin-containing monooxygenase family protein) [NCBI Gene 841313] {aka F27K7.7, F27K7_7, YUCCA 10}, YUC1 (Flavin-binding monooxygenase family protein) [NCBI Gene 829389] {aka L23H3.20, L23H3_20, YUC, YUCCA, YUCCA 1}
- **Chemicals:** chl (-), IAA (MESH:C030737), Auxin (MESH:D007210), Chl (MESH:D002734)
- **Species:** Arabidopsis thaliana (mouse-ear cress, species) [taxon 3702], Coffea arabica (arabica coffee, species) [taxon 13443], Vitis vinifera (wine grape, species) [taxon 29760]

## Full text

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## Figures

5 figures with captions in the complete paper: https://tomesphere.com/paper/PMC12930011/full.md

## References

70 references — full list in the complete paper: https://tomesphere.com/paper/PMC12930011/full.md

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Source: https://tomesphere.com/paper/PMC12930011