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k Bilin Metabolism in Advanced article Article Contents Plants: Structure, • Introduction • Biosynthesis of Bilins Function and Haem • Phytochromobilin (PB) • Phycocyanobilin (PCB) Oxygenase Regulation of • Phycoerythrobilin (PEB) • Phycourobilin (PUB) Bilin Biosynthesis • HO Regulation in Bilin Biosynthesis • Biochemistry of Bilins Gyan Singh Shekhawat, Plant Biotechnology and Molecular Biology Labora- • Physiological Role of Bilins in Photosynthetic Organisms tory, Department of Botany, JNV University, Jodhpur, Rajasthan, India • Transcription Factors Involved in Bilin Signalling Suman Parihar, Plant Biotechnology and Molecular Biology Laboratory, Depart- • Phyllobilins – An Overlooked Class of Naturally Occurring Linear Tetrapyrroles ment of Botany, JNV University, Jodhpur, Rajasthan, India • Phyllobilins vs Bilins Lovely Mahawar, Plant Biotechnology and Molecular Biology Laboratory, • Conclusion and Future Prospects Department of Botany, JNV University, Jodhpur, Rajasthan, India Online posting date: 17th April 2019 Khushboo Khator, Plant Biotechnology and Molecular Biology Laboratory, Department of Botany, JNV University, Jodhpur, Rajasthan, India Neha Bulchandani, Plant Biotechnology and Molecular Biology Laboratory, Department of Botany, JNV University, Jodhpur, Rajasthan, India Bilins are open-chain tetrapyrroles with a wide structure and functions of bilins, this article k range of visible and nearly visible-light absorption also aims to recapitulate and discuss the current k and emission properties. The linear tetrapyr- progress in the field of bilins and to emphasise the role molecules function as chromophores of emerging areas. the light-harvesting phycobiliproteins and phytochrome-mediated light sensing in pho- tosynthetic organisms. They are derived from Introduction the cyclic precursor haem. The initial step in bilin biosynthesis is the conversion of haem into Bilins (bilichrome) are open-chain tetrapyrroles extensively dis- biliverdin (BV IX ) catalysed by haem oxygenase, tributed in all organisms excluding Archaea. They are biologi- which is subsequently reduced to specific bilins cal pigments formed as a metabolic product of protoporphyrin IX and execute several functions in different life forms. Com- by ferredoxin-dependent bilin reductases (FDBRs). monly, biosynthesis of linear tetrapyrroles is catabolic in nature Bilins usually bound to apoproteins via single or and related to iron acquisition from haem but in phototrophs, double covalent bonds to form a macromolecu- it is an anabolic process (Zhang et al., 2018). In phototrophs, lar complex phycobilisomes. The attachment of bilins act as a protein cofactor with light-sensing (phytochromes) apoproteins to bilin is an autocatalytic process, and light-harvesting (phycobiliproteins) properties. This unique but bilin lyases are required for the specific property is due to the presence of a chromophore-conjugated attachment of bilin chromophores to phyco- double-bond system, which absorbs photons of different wave- biliprotein apoproteins. Besides the biosynthesis, lengths. Distinct degrees of conjugation result in absorption of different ranges of light. Moreover, bilins are essential pig- ments in a number of photoperiodic processes in green plants eLS subject area: Plant Science and act as accessory pigments during the photosynthesis of red algae. As accessory pigments, bilins absorb wavelengths of How to cite: light, which are not absorbed by chlorophyll. In nature, approx- Shekhawat, Gyan Singh; Parihar, Suman; Mahawar, Lovely; imately all open-chain tetrapyrroles are the derivatives of haem Khator, Khushboo; and Bulchandani, Neha (April 2019) Bilin Metabolism in Plants: Structure, Function and Haem except preuroporphyrinogen (hydroxymethylbilane), an interme- Oxygenase Regulation of Bilin Biosynthesis. In: eLS. John Wiley diate of porphyrin biosynthesis. Hence, formation of bilin is & Sons, Ltd: Chichester. directly related to haem and chlorophyll synthesis. The prelim- DOI: 10.1002/9780470015902.a0028352 inary step in bilin biosynthesis is formation of an open-chain eLS © 2019, John Wiley & Sons, Ltd. www.els.net 1 k k Bilin Metabolism in Plants: Structure, Function and Haem Oxygenase Regulation of Bilin Biosynthesis tetrapyrrole, Biliverdin IX α catalysed by an enzyme haem oxy- controlled by a series of enzymes (Terry, 1997). The prelimi- genase (Shekhawat and Verma, 2010; Mahawar and Shekhawat, nary reaction in the PΦB synthesis is the formation of haem and 2018). chlorophyll. A key step in the reaction is the formation of proto- Haem oxygenases (HOs; EC 1.14.99.3) are a highly active fam- porphyrin IX (cyclic bilin), which either synthesises haem by the ily of universal antioxidant enzymes, which catalyse the oxidative insertion of Fe+2 ion via ferrochelatase or diverts towards chloro- degradation of Fe (III) protoporphyrin IX (haem) to biliverdin, phyll lineage by Mg+2 chelatase enzyme (Papenbrock et al., ferrous ion and carbon monoxide in the presence of reducing 2000) (Figure 1). The rate-determining step in the PΦB pathway equivalents (Balestrasse et al., 2005; Shekhawat and Verma, is the oxidative degradation of haem to biliverdin IXa (BV) by 2010). The enzyme was initially identified in animals by Ten- an enzyme haem oxygenase (HO) (Muramoto et al., 2002). BV hunen et al. (1969) as an elementary enzyme that produces biliru- is further reduced to phytochromobilin by PΦB synthase/HY 2 bin by the reduction of biliverdin through biliverdin reductase. reductase to form 3(Z)-PΦB, and finally, 3(Z)-PΦB is isomerised Besides animals, the enzyme is found in pathogenic bacteria, to 3(E)-PΦB. Less literature is available about the isomerisa- algae (both lower and higher), cyanobacteria, cryptophytes and tion of 3(Z) to 3(E) and whether it is spontaneous or enzymatic higher plants. Haem oxygenase performs various functions in (Figure 1). different organisms, but the haem degradation process is simi- lar in all organisms. In higher plants, genes of haem oxygenase have been documented in several angiosperms, gymnosperms and Phycocyanobilin (PCB) mosses. HO in plants comprises of a small gene family of four members, which is subsequently divided into two subfamilies. Phycocyanobilin (blue coloured), one of the major copious One subfamily consists of HY1 (HO 1), HO 3 and HO 4, while bilin acts as a light-harvesting pigment in blue-green algae, the other one only contains HO 2. Both subfamilies are soluble rhodophytes, glaucophytes and cryptophytes. Moreover, in and located in the chloroplast (Emborg et al., 2006). blue-green and streptophyte algae, PCB also functions as the chromophore of phytochrome (Rockwell et al., 2017). Phycocyanobilin is synthesised by two diverse enzymes. In Biosynthesis of Bilins cyanophages and blue-green algae, phycocyanobilin: ferredoxin oxidoreductase (PcyA; EC: 1.3.7.5) requires four electrons to Bilins are open-chain tetrapyrroles derived from the cyclic pre- catalyse the reduction of BV to PCB via a two-step process. The cursor haem. The preliminary reaction in the bilin biosynthesis first step of the reaction yields an intermediate 181,182 dihydro- k is the ring opening of haem porphyrin to open-chain tetrapyrrole biliverdin by the two-electron reduction mediated by PcyA. In the k biliverdin (BV IX α) arbitrated by haem oxygenases (Cornejo and second step, PcyA uses remaining two electrons to reduce 181, Beale, 1988). The BV IX α is then reduced to light-sensing or 182 dihydrobiliverdin into phycocyanobilin (Figure 1). Recently, light-harvesting pigments by ferredoxin-dependent bilin reduc- Rockwell et al. (2017) illustrated the bilin biosynthetic pathway tases (FDBRs). FDBRs are versatile enzymes that catalyse the of algae Klebsormidium flaccidum in Escherichia coli by observ- synthesis of a broad variety of pigments. Different FDBRs are ing the co-expression of HY2 reductase (Kfla HY2) with HO found in different photosynthetic organisms to produce vari- (KflaHY1) and synthesises functional holophytochromes using ous types of bilins including phytochromobilin (PΦB), phyco- PCB as the chromophore (Rockwell et al., 2017). cyanobilin (PCB), phycoerythrobilin (PEB) and phycourobilin (PUB) (Zhang et al., 2018). FDBR family comprises of six mem- bers and subdivided into two discrete groups, which depend on Phycoerythrobilin (PEB) the number of electron transfer during the biosynthesis. The reductases 15, 16-dihydrobiliverdin: ferredoxin oxidoreductase The pink open-chain tetrapyrrole phycoerythrobilin is a signifi- (PebA; EC: 1.3.7.2), PebB and HY2 from higher plants catal- cant light-harvesting pigment in phycobiliproteins of blue-green yse two-electron reduction. While phycocyanobilin:ferredoxin algae, rhodophytes, glaucophytes and cryptomonads. Depend- oxidoreductase (PcyA; EC: 1.3.7.5), phycoerythrobilin synthase ing on the origin of ferredoxin-dependent biliverdin reductase (PebS; EC: 1.3.7.6) and phycourobilin synthase (PUBS; EC: not (FDBR), there are two different pathways to synthesise PEB. The designated yet) are able to catalyse two-electron reduction in two first pathway occurs in cyanobacteria, in which the reductase pair subsequent steps. Initially, the reductases transfer two electrons PebA and PebB is involved in the synthesis of phycoerythrobilin. to the substrate BV to form an intermediate dihydrobiliverdin The initial step of this pathway yields an intermediate 15, 16 (DHBV), which is subsequently reduced to tetrahydrobiliverdin dihydrobiliverdin by a two-electron reduction of biliverdin catal- in the second
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