Chlorophyll Degradation and Its Physiological Function
Open accessAbstract
Research on chlorophyll degradation has progressed significantly in recent decades. In the 1990s, the structure of linear tetrapyrrole, which is unambiguously a chlorophyll degradation product, was determined. From the 2000s until the 2010s, the major enzymes involved in chlorophyll degradation were identified, and the pheophorbide a oxygenase/phyllobilin pathway was established. This degradation pathway encompasses several steps: (i) initial conversion of chlorophyll b to 7-hydroxymethyl chlorophyll a, (ii) conversion of 7-hydroxymethyl chlorophyll a to chlorophyll a, (iii) dechelation of chlorophyll a to pheophytin a, (iv) dephytylation of pheophytin a to pheophorbide a, (v) opening of the macrocycle to yield a red chlorophyll catabolite (RCC) and (vi) conversion of RCC to phyllobilins. This pathway converts potentially harmful chlorophyll into safe molecules of phyllobilins, which are stored in the central vacuole of terrestrial plants. The expression of chlorophyll-degrading enzymes is mediated by various transcription factors and influenced by light conditions, stress and plant hormones. Chlorophyll degradation is differently regulated in different organs and developmental stages of plants. The initiation of chlorophyll degradation induces the further expression of chlorophyll-degrading enzymes, resulting in the acceleration of chlorophyll degradation. Chlorophyll degradation was initially considered the last reaction in senescence; however, chlorophyll degradation plays crucial roles in enhancing senescence, degrading chlorophyll–protein complexes, forming photosystem II and maintaining seed quality. Therefore, controlling chlorophyll degradation has important agricultural applications.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
A classical Mendel mutation leads to a stay-green phenotype in pea seed cotyledons and encodes a Mg2+-dechelatase that converts chlorophyll to pheophytin by removal of the central Mg atom.
“One of the classical mutations used by Gregor Mendel during his studies of inheritance leads to a “stay-green” phenotype in pea seed cotyledons and encodes a Mg2+-dechelatase that converts chlorophyll to pheophytin by removal of the central Mg atom.85”
From Metals in Motion: Understanding Labile Metal Pools in Bacteria (2025) · cites this paper as [85]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
No references could be resolved yet.
Research works printed but not linked: 7
- Delmas, F., Sankaranarayanan, S., Deb, S., Widdup, E., Bournonville, C., Bol- lier, N., et al. (2013) ABI3 controls embryo degreening through Mendel's I locus. Proc. Natl. Acad. Sci. U. S. A. 110: E3888-E3894.
- Kashiyama, Y., Yokoyama, A., Kinoshita, Y., Shoji, S., Miyashiya, H., Shiratori, T., et al. (2012) Ubiquity and quantitative significance of detoxification catabolism of chlorophyll associated with protistan herbivory. Proc. Natl. Acad. Sci. U. S. A. 109: 17328-17335.
- Mach, J.M., Castillo, A.R., Hoogstraten, R. and Greenberg, J.T. (2001) The Arabidopsis accelerated cell death gene ACD2 encodes red chlorophyll catabolite reductase and suppresses the spread of disease symptoms. Proc. Natl. Acad. Sci. U. S. A. 98: 771-776.
- Oberhuber, M., Berghold, J., Breuker, K., Hortensteiner, S. and Krautler, B. (2003) Breakdown of chlorophyll: a nonenzymatic reaction accounts for the formation of the colorless "nonfluorescent" chlorophyll catabolites. Proc. Natl. Acad. Sci. U. S. A. 100: 6910-6915.
- Pruzinska, A., Tanner, G., Anders, I., Roca, M. and Hörtensteiner, S. (2003) Chlorophyll breakdown: pheophorbide a oxygenase is a Rieske-type iron-sulfur protein, encoded by the accelerated cell death 1 gene. Proc. Natl. Acad. Sci. U. S. A. 100: 15259-15264.
- Sato, Y., Morita, R., Nishimura, M., Yamaguchi, H. and Kusaba, M. (2007) Mendel's green cotyledon gene encodes a positive regulator of the chlorophyll-degrading pathway. Proc. Natl. Acad. Sci. U. S. A. 104: 14169-14174.
- Wang, L., Kim, C., Xu, X., Piskurewicz, U., Dogra, V., Singh, S., et al. (2016) Singlet oxygen-and EXECUTER1-mediated signaling is initiated in grana margins and depends on the protease FtsH2. Proc. Natl. Acad. Sci. U. S. A. 113: E3792-E3800.
Cited by
Sorted by citations
Metals in Motion: Understanding Labile Metal Pools in Bacteria
Helmann, J. D. (2025) · Biochemistry · doi:10.1021/acs.biochem.4c00726 · Cited by 49 · see citing works
- Authors
- Tanaka, A., & Ito, H.
- Affiliations
- Hokkaido University (JP)
- Institute of Low Temperature Science, Hokkaido University , N19 W8, Sapporo, Hokkaido, 060-0819
- ORCID
- Ito, Hisashi
- Venue
- Plant And Cell Physiology
- Publisher
- Oxford University Press (OUP)
- Published
- 2024-08-22
- Volume
- 66
- Issue
- 2
- Pages
- 139-152
- ISSN
- 0032-0781 (ISSN-L)
- 1471-9053
- OpenAlex
- W4401835062
- Cited by
- 143
- References
- 0
- Citations by year
- 2026: 93 · 2025: 46 · 2024: 4
- FWCI
- 5.63
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Locations
- Plant and Cell Physiology (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Japan Society for the Promotion of Science (23K05691)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Plant Gene Expression Analysis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Photosynthetic Processes and Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Plant biochemistry and biosynthesis
- Keywords
- chlorophyll degradation, pheophorbide a oxygenase, pheophytin a, chlorophyll-protein complexes, leaf senescence, photosystem II, seed quality, transcription factors, light regulation, plant hormones, stress response, vacuolar storage, tetrapyrroles
- MeSH terms
- Chlorophyll, Oxygenases, Plants
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review