Cited by 143Plant Gene Expression AnalysisPhotosynthetic Processes and MechanismsPlant biochemistry and biosynthesis

Chlorophyll Degradation and Its Physiological Function

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Tanaka, Ayumi, Ito, Hisashi·2025·Plant And Cell Physiology

Abstract

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.

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  • 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”

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  1. 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.
  2. 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.
  3. 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.
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  5. 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.
  6. 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.
  7. 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.

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Authors
Tanaka, A., & Ito, H.
Affiliations
  • Hokkaido University (JP)
  • Institute of Low Temperature Science, Hokkaido University , N19 W8, Sapporo, Hokkaido, 060-0819
Venue
Plant And Cell Physiology
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
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

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