Light dependent protochlorophyllide oxidoreductase: a succinct look.

Chlorophyll biosynthesis Light-dependent protochlorophyllide oxidoreductase Photooxidative damage Prolamellar body

Journal

Physiology and molecular biology of plants : an international journal of functional plant biology
ISSN: 0971-5894
Titre abrégé: Physiol Mol Biol Plants
Pays: India
ID NLM: 101304333

Informations de publication

Date de publication:
May 2024
Historique:
received: 10 11 2023
revised: 01 03 2024
accepted: 29 04 2024
pmc-release: 01 05 2025
medline: 7 6 2024
pubmed: 7 6 2024
entrez: 7 6 2024
Statut: ppublish

Résumé

Reducing protochlorophyllide (Pchlide) to chlorophyllide (Chlide) is a major regulatory step in the chlorophyll biosynthesis pathway. This reaction is catalyzed by light-dependent protochlorophyllide oxidoreductase (LPOR) in oxygenic phototrophs, particularly angiosperms. LPOR-NADPH and Pchlide form a ternary complex to be efficiently photo-transformed to synthesize Chlide and, subsequently, chlorophyll during the transition from skotomorphogenesis to photomorphogenesis. Besides lipids, carotenoids and poly-cis xanthophylls influence the formation of the photoactive LPOR complexes and the PLBs. The crystal structure of LPOR reveals evolutionarily conserved cysteine residues implicated in the Pchlide binding and catalysis around the active site. Different isoforms of LPOR viz PORA, PORB, and PORC expressed at different stages of chloroplast development play a photoprotective role by quickly transforming the photosensitive Pchlide to Chlide. Non-photo-transformed Pchlide acts as a photosensitizer to generate singlet oxygen that causes oxidative stress and cell death. Therefore, different isoforms of LPOR have evolved and differentially expressed during plant development to protect plants from photodamage and thus play a pivotal role during photomorphogenesis. This review brings out the salient features of LPOR structure, structure-function relationships, and ultra-fast photo transformation of Pchlide to Chlide by oligomeric and polymeric forms of LPOR.

Identifiants

pubmed: 38846463
doi: 10.1007/s12298-024-01454-5
pii: 1454
pmc: PMC11150229
doi:

Types de publication

Journal Article Review

Langues

eng

Pagination

719-731

Informations de copyright

© Prof. H.S. Srivastava Foundation for Science and Society 2024. Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law.

Déclaration de conflit d'intérêts

Conflict of interestThe authors declare that they have no known conflicting interest.

Auteurs

Pratishtha Vedalankar (P)

School of Life Sciences, Jawaharlal Nehru University, New Delhi, 110067 India.

Baishnab C Tripathy (BC)

Department of Biotechnology, Sharda University, Greater Noida, Uttar Pradesh 201310 India.

Classifications MeSH