Light Dependent Protochlorophyllide Oxidoreductase: a Succinct Look

Overview

Journal Physiol Mol Biol Plants

Specialty Biology

Date 2024 Jun 7

PMID 38846463

Authors

Pratishtha Vedalankar

Baishnab C Tripathy

Affiliations

Soon will be listed here.

Abstract

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.

References

Horton P, Leech R . The Effect of ATP on the Photoconversion of Protochlorophyllide in Isolated Etioplasts of Zea mays. Plant Physiol. 1975; 56(1):113-20. PMC: 541309. DOI: 10.1104/pp.56.1.113. View

Spano A, He Z, Michel H, Hunt D, Timko M . Molecular cloning, nuclear gene structure, and developmental expression of NADPH: protochlorophyllide oxidoreductase in pea (Pisum sativum L.). Plant Mol Biol. 1992; 18(5):967-72. DOI: 10.1007/BF00019210. View

Heyes D, Hunter C . Site-directed mutagenesis of Tyr-189 and Lys-193 in NADPH: protochlorophyllide oxidoreductase from Synechocystis. Biochem Soc Trans. 2002; 30(4):601-4. DOI: 10.1042/bst0300601. View

Takio S, Nakao N, Suzuki T, Tanaka K, Yamamoto I, Satoh T . Light-dependent expression of protochlorophyllide oxidoreductase gene in the liverwort, Marchantia paleacea var. diptera. Plant Cell Physiol. 1998; 39(6):665-9. DOI: 10.1093/oxfordjournals.pcp.a029420. View

Wang L, Apel K . Dose-dependent effects of 1O2 in chloroplasts are determined by its timing and localization of production. J Exp Bot. 2018; 70(1):29-40. PMC: 6939833. DOI: 10.1093/jxb/ery343. View

Engdahl S, ARONSSON H, Sundqvist C, Timko M, Dahlin C . Association of the NADPH:protochlorophyllide oxidoreductase (POR) with isolated etioplast inner membranes from wheat. Plant J. 2001; 27(4):297-304. DOI: 10.1046/j.1365-313x.2001.01094.x. View

Schoefs B, Franck F . Protochlorophyllide reduction: mechanisms and evolutions. Photochem Photobiol. 2004; 78(6):543-57. DOI: 10.1562/0031-8655(2003)078<0543:prmae>2.0.co;2. View

Osborne A, Osagiede A, Storm A, Hulse-Kemp A, Stoeckman A . gene of unknown function Gohir.A03G0737001 encodes a potential Chaperone-like Protein of protochlorophyllide oxidoreductase (CPP1). MicroPubl Biol. 2023; 2023. PMC: 10423991. DOI: 10.17912/micropub.biology.000867. View

Solymosi K, Mysliwa-Kurdziel B . The Role of Membranes and Lipid-Protein Interactions in the Mg-Branch of Tetrapyrrole Biosynthesis. Front Plant Sci. 2021; 12:663309. PMC: 8113382. DOI: 10.3389/fpls.2021.663309. View

10.

Darrah P, Kay S, Teakle G, Griffiths W . Cloning and sequencing of protochlorophyllide reductase. Biochem J. 1990; 265(3):789-98. PMC: 1133702. DOI: 10.1042/bj2650789. View

11.

WILKS H, Timko M . A light-dependent complementation system for analysis of NADPH:protochlorophyllide oxidoreductase: identification and mutagenesis of two conserved residues that are essential for enzyme activity. Proc Natl Acad Sci U S A. 1995; 92(3):724-8. PMC: 42692. DOI: 10.1073/pnas.92.3.724. View

12.

Sameer H, Victor G, Katalin S, Henrik A . Elucidation of ligand binding and dimerization of NADPH:protochlorophyllide (Pchlide) oxidoreductase from pea (Pisum sativum L.) by structural analysis and simulations. Proteins. 2021; 89(10):1300-1314. DOI: 10.1002/prot.26151. View

13.

Kaneko T, Sato S, Kotani H, Tanaka A, Asamizu E, Nakamura Y . Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions. DNA Res. 1996; 3(3):109-36. DOI: 10.1093/dnares/3.3.109. View

14.

Benli M, Schulz R, Apel K . Effect of light on the NADPH-protochlorophyllide oxidoreductase of Arabidopsis thaliana. Plant Mol Biol. 1991; 16(4):615-25. DOI: 10.1007/BF00023426. View

15.

Armstrong G, Runge S, Frick G, Sperling U, Apel K . Identification of NADPH:protochlorophyllide oxidoreductases A and B: a branched pathway for light-dependent chlorophyll biosynthesis in Arabidopsis thaliana. Plant Physiol. 1995; 108(4):1505-17. PMC: 157530. DOI: 10.1104/pp.108.4.1505. View

16.

Taylor A, Zhang S, Johannissen L, Sakuma M, Phillips R, Green A . Mechanistic implications of the ternary complex structural models for the photoenzyme protochlorophyllide oxidoreductase. FEBS J. 2023; 291(7):1404-1421. DOI: 10.1111/febs.17025. View

17.

Reinbothe C, El Bakkouri M, Buhr F, Muraki N, Nomata J, Kurisu G . Chlorophyll biosynthesis: spotlight on protochlorophyllide reduction. Trends Plant Sci. 2010; 15(11):614-24. DOI: 10.1016/j.tplants.2010.07.002. View

18.

Fujita Y, Takagi H, Hase T . Cloning of the gene encoding a protochlorophyllide reductase: the physiological significance of the co-existence of light-dependent and -independent protochlorophyllide reduction systems in the cyanobacterium Plectonema boryanum. Plant Cell Physiol. 1998; 39(2):177-85. DOI: 10.1093/oxfordjournals.pcp.a029355. View

19.

Masuda S, Ikeda R, Masuda T, Hashimoto H, Tsuchiya T, Kojima H . Prolamellar bodies formed by cyanobacterial protochlorophyllide oxidoreductase in Arabidopsis. Plant J. 2009; 58(6):952-60. DOI: 10.1111/j.1365-313X.2009.03833.x. View

20.

Pattanayak G, Tripathy B . Overexpression of protochlorophyllide oxidoreductase C regulates oxidative stress in Arabidopsis. PLoS One. 2011; 6(10):e26532. PMC: 3198771. DOI: 10.1371/journal.pone.0026532. View