Photorespiration: current status and approaches for ... - iGRAD-Plant

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Photorespiration: current status and approaches for metabolic 

engineering 

Veronica G Maurino 1 and Christoph Peterhansel 2 

Photorespiration results from the oxygenase reaction catalysed 

by ribulose-1,5-bisphosphate carboxylase/oxygenase and 

serves as a carbon recovery system. It comprises enzymatic 

reactions distributed in chloroplasts, peroxisomes and 

mitochondria. The recent discovery of a cytosolic bypass and 

the requirement of complex formation between some 

photorespiratory proteins added additional levels of complexity 

to the known pathway. Photorespiration may have evolved in 

both, C 3 and C 4 plants, to prevent an accumulation of toxic 

levels of glycolate. Moreover, it is suggested that 

photorespiration evolved in cyanobacteria before the origin of 

chloroplasts. Synthetic detours, reminiscent of secondary 

photorespiratory pathways naturally occurring in 

cyanobacteria, were installed in Arabidopsis thaliana to bypass 

photorespiration. An enrichment of CO2 in the chloroplast and 

positive effects on plant growth raised the question why these 

pathways have been lost from higher plants. 

Addresses 

1 

Botanisches Institut, Universität zuKöln, Zülpicher Str. 47b, 50674 

Cologne, Germany 

2 

Institut für Botanik, Leibniz-Universität Hannover, Herrenhäuserstr. 2, 

30419 Hannover, Germany 

Corresponding author: Maurino, Veronica G (v.maurino@uni-koeln.de) 

and Peterhansel, Christoph (cp@botanik.uni-hannover.de) 

Current Opinion in Plant Biology 2010, 13:249–256 

This review comes from a themed issue on 

Physiology and metabolism 

Edited by Uwe Sonnewald and Wolf B. Frommer 

Available online 23rd February 2010 

1369-5266/$ – see front matter 

# 2010 Elsevier Ltd. All rights reserved. 

DOI 10.1016/j.pbi.2010.01.006 

Introduction 

Plant photosynthetic carbon metabolism is composed of 

two connected pathways: the reductive photosynthetic 

carbon metabolism, also known as the C3 or Calvin 

cycle, and the oxidative photosynthetic carbon metabolism, 

also known as the C2 cycle or photorespiratory 

pathway (Figure 1). Both cycles are initiated by the action 

of ribulose-1,5-bisphosphate carboxylase/oxygenase 

(RubisCO) on ribulose-1,5-bisphosphate (RubP). Carboxylation 

of RubP yields 3-phosphoglycerate (3-PGA), 

while its oxygenation leads to the synthesis of one molecule 

of 3-PGA and one molecule of 2-phosphoglycolate 

(2-PG). The 3-PGA/2-PG ratio is determined by the 

CO2/O2 ratio in the chloroplast and the CO2/O2 specificity 

factor of RubisCO (V = VC/VO = VC/KC KO/VO [CO2]/ 

[O2], where KC and KO represent the Michaelis Menten 

constants for CO2 and O2, and VC and VO the maximal 

velocities for carboxylation and oxygenation), which 

indicates the preference of the enzyme for CO2 over O2 

and varies between species. The photorespiratory C2 cycle 

serves as a carbon recovery system converting 2-PG to 3- 

PGA that can re-enter the reductive cycle. This pathway is 

coordinated between four cellular compartments and uses 

a multitude of enzymes and transport processes (Figure 1). 

Current status of the photorespiratory 

pathway in the model plant Arabidopsis 

thaliana 

Chloroplastic production of glycolate and its 

peroxisomal conversion into glycine 

First, 2-PG is dephosphorylated in the chloroplasts 

through 2-phosphoglycolate phosphatase (PGLP) and 

the glycolate produced is transported to peroxisomes 

for further metabolization (Figure 1). A. thaliana (Arabidopsis) 

possesses two genes encoding active PGLPs, but 

only PGLP1 (At5g36700) participates in photorespiraton 

[1]. Knock-out mutants of this gene have very low leaf 

PGLP activity and cannot survive in normal air but grow 

well in a CO2-enriched environment where photorespiration 

is low [1]. 

In the peroxisomes, glycolate oxidase (GO) catalyses the 

oxidation of glycolate into equimolar amounts of glyoxylate 

and H 2O 2. Catalase (CAT) degrades H 2O 2 and 

glutamate:glyoxylate aminotransferase (GGAT) transaminates 

glyoxylate into glycine, which is further transported 

to the mitochondria (Figure 1). GO-suppressed 

rice showed the typical conditional lethal high-CO2requiring 

phenotype [2]. Moreover, GO was found to 

exert a strong regulation over photosynthesis, possible 

through a feedback inhibition on RubisCO activase [2]. 

Arabidopsis has two genes encoding peroxisomal glutamate:glyoxylate 

aminotransferase (GGAT1, At1g23310 

and GGAT2, At1g70580) shown to participate in photorespiration 

[3,4]. Knock-out mutants of GGAT1 showed a 

weak residual GGAT activity, repressed growth in normal 

air and high light intensity, but normal growth at elevated 

CO2 conditions [4]. This partial photorespiratory phenotype 

suggests that both, GGAT1 and GGAT2, may 

contribute to photorespiration. However, GGAT1 is 

highly expressed in both leaves and roots, indicating that 

its function is not restricted to photorespiration. 

www.sciencedirect.com Current Opinion in Plant Biology 2010, 13:249–256

250 Physiology and metabolism 

Figure 1 

The photorespiratory carbon and nitrogen cycle comprises enzymes and transporters distributed between chloroplasts, peroxisomes, mitochondria 

and cytosol. DiT1 and DiT2: dicarboxylate transporter 1 and 2, are the only transporters identified at the genomic level [33,34]. CAT: catalase; GDC: 

glycine decarboxylase; GGAT: glutamate:glyoxylate aminotransferase; GLYK: glycerate kinase; GO: glycolate oxidase; GOGAT: 

glutamate:oxoglutarate aminotransferase; GS: glutamine synthetase; HPR1: peroxisomal hydroxypyruvate reductase; HPR2: cytosolic 

hydroxypyruvate reductase; PGP: phosphoglycolate phosphatase; RubisCO: ribulose-1,5-bisphosphate carboxylase/oxygenase; RubP: ribulose-1,5bisphosphate; 

SGAT: serine-glutamate aminotransferase; SHMT: serine hydroxymethyl transferase; THF: tetrahydrofolate; 5,10-CH 2-THF: 5,10methylene-THF; 

3-PGA: 3-phosphoglycerate. The dashed line represents many enzymatic steps. 

Mitochondrial conversion of glycine into serine and the 

need for ammonia re-assimilation 

In the mitochondria, glycine is decarboxylated and deaminated 

by the glycine decarboxylase complex (GDC) 

yielding CO 2,NH 4 + , NADH and 5,10-methylene tetrahydrofolate. 

The latter is used by serine hydroxymethyltransferase 

(SHMT) to synthesize serine by transferring 

the activated C 1 unit onto another molecule of glycine 

(Figure 1). 

GDC is a hetero-tetramer and Arabidopsis possesses two 

genes each encoding for P (At4g33010 and At2g26080) 

and L (At3g17240 and At1g48030) proteins, three genes 

for H (At2g35370, At2g35120 and At1g32470) proteins 

and one gene for the T (At1g11860) protein [5]. Only few 

T-DNA-tagged mutants in these genes were analysed 

until present. Recent studies showed that individual 

knock-outs of the P-protein genes grow normally [6]. 

In contrast, the combined knock-out of both genes 

is lethal even at non-photorespiratory conditions providing 

evidence that the GDC reaction cannot be bypassed 

[6]. GDC seems to be indispensable at least for onecarbon 

metabolism (Figure 2), by recycling glycine originated 

from extramitochondrial SHMT. In Arabidopsis, 

Current Opinion in Plant Biology 2010, 13:249–256 www.sciencedirect.com

Figure 2 

Simplified scheme illustrating the connection of C 1-metabolism to the photorespiratory carbon cycle. 

At4g37930 encodes the photorespiratory SHMT1 as 

knock-out mutants in this SHMT gene are lethal at 

ambient CO2 levels but grow normally at high CO2 [7]. 

In the course of the GDC reaction, one-quarter of the 

bound carbon is lost as photorespiratory CO2 and an 

equimolar amount of NH4 + is released, which needs to 

be re-assimilated through the glutamine synthetase (GS)/ 

ferredoxin-dependent glutamate:oxoglutarate aminotransferase 

(Fd-GOGAT) cycle [8]. The relevance of this 

nitrogen re-assimilation pathway was recently confirmed 

as mutants in Fd-GOGAT (At5g04140) displayed a 

typical photorespiratory phenotype [9 ]. 

Peroxisomal production of glycerate and its 

chloroplastic phosphorylation into 3-PGA 

Glycine generated in the mitochondria is transported to 

the peroxisomes where it is converted to glycerate 

through the sequential action of serine:glyoxylate aminotransferase 

(SGAT) and hydroxypyruvate reductase 

(HPR1; Figure 1). SGAT is encoded by a single gene 

Photorespiration Maurino and Peterhansel 251 

in Arabidopsis (At2g13360) and its disruption results in 

plants that are unviable under normal atmospheric conditions 

[10]. On the contrary, disruption of HPR1 

(At1g68010) caused negligible effects on growth in normal 

air indicating the existence of an alternative reaction 

[11 ] (see below). 

The transport of glycerate to the chloroplasts and its 

phosphorylation to 3-PGA by D-glycerate 3-kinase 

(GLYK) completes the photorespiratory pathway 

(Figure 1). In Arabidopsis, GLYK is encoded by a 

single-copy gene (At1g80380). Loss of its function results 

in plants that are not viable in normal air [12]. Plant 

GLYKs represent a novel protein family as they are 

structurally and phylogenetically different from known 

GLYKs from non-photosynthetic organisms [12]. 

Alternative photorespiratory reactions 

In a recent publication, Timm et al. [11 ] presented 

biochemical and genetic evidence that HPR2 

(At1g79870) is the cytosolic enzyme that provides a 



bypass to the peroxisomal conversion of glycine into 

glycerate (Figure 1). This reaction serves as a mechanism 

for the utilization of hydroxypyruvate leaking from the 

peroxisomes and extends the photorespiratory pathway to 

the cytosolic compartment. In line with this, combined 

deletion of the peroxisomal and cytosolic reactions is 

detrimental to air-grown mutants [11 ]. 

Most green algae convert glycolate to glycerate in the 

mitochondrium [13]. Knock-out of glycolate dehydrogenase 

(GlyDH), the first enzyme in this pathway, in Chlamydomonas 

results in a high-CO2-requiring phenotype 

[14]. It has been suggested that this mitochondrial pathway 

is conserved in higher plants, because an Arabidopsis 

protein with homology to Chlamydomonas GlyDH is 

targeted to mitochondria [15] and insertion mutants 

showed altered photorespiratory properties albeit not 

being affected in growth [16]. This view has been 

recently challenged by characterization of the Arabidopsis 

homolog enzyme [17 ], which shows a much higher preference 

for D-lactate compared to glycolate because of an 

extremely low catalytic rate with the latter substrate. 

Moreover, this enzyme was shown to participate in planta 

in the methylglyoxal pathway [17 ], suggesting that the 

ancient photorespiratory pathway has been re-directed to 

a new function in higher plants. 

Complex regulation of the mitochondrial reactions of 

photorespiration 

Recently, Jamai et al. [9 ] reported that Fd-GOGAT, a 

component of the photorespiratory nitrogen assimilation 

cycle in the chloroplast, is dual targeted to the mitochondria. 

Here, the protein seemingly does not exert an 

enzymatic function, but rather associates with SHMT1. 

Furthermore, two 10-formyl THF deformylases (10- 

FDF; At4g17360 and At5g47435), components of the 

mitochondrial THF cycle, were shown to be essential 

for photorespiration as they oppose the accumulation of 

5-formyl THF ([Figure 2]) [18 ]. This compound 

is synthesized by SHMT in a side reaction using 

5,10-methenyl-THF as substrate and is a strong inhibitor 

of the SHMT activity. It was speculated that the role of 

Fd-GOGAT bound to SHMT1 might be to reduce the 

sensitivity of SHMT1 to 5-formyl THF or to inhibit its 

accumulation [9 ]. 

Why photorespiration? 

Photorespiration lowers photosynthetic efficiency in that 

CO2 and ammonia should be re-assimilated with the 

concomitant consumption of both ATP and reducing 

power [19]. So why photorespiration? Although the main 

function of photorespiration would be the recovery of 

carbon diverted by the oxygenase activity of RubisCO 

some other functions have also been proposed. By transporting 

excess reducing equivalents from the chloroplast 

photorespiration may be a mechanism for preventing the 

over reduction of the stroma, and thus photoinhibition, as 

occurs under high light, drought and salt-stress and CO2free 

air [19,20]. This transfer of reducing equivalents 

might also be important for nitrate assimilation [21]. 

Moreover, photorespiration would be important for avoiding 

the suppression of the repair of photodamaged photosystem 

II, as different photorespiratory mutants of 

Arabidopsis showed inhibition of the synthesis of the 

D1 protein at the level of translation [22]. Finally, through 

H2O2 production and pyridine nucleotide interactions, 

photorespiration makes a key contribution to cellular 

redox homeostasis [23]. 

Photorespiration is required in all 

photosynthetic organisms 

The dual function of RubisCO is common to all photosynthetic 

organisms [24]. It is therefore plausible to 

assume that all photosynthetic organisms also require a 

pathway for phosphoglycolate conversion. According to 

this, genes encoding photorespiratory enzymes are found 

throughout the green lineage [13,25]. However, cyanobacteria, 

algae and higher plants developed mechanisms 

for the concentration of CO2 around RubisCO resulting in 

an efficient suppression of phosphoglycolate production 

(Figure 3). It was assumed that these organisms do not 

strictly require photorespiration. Two recent papers have 

now falsified this hypothesis. In the first study, Zelitch 

et al. [26 ] isolated a maize mutant with a transposon 

integration in the GO1 gene that encodes the major 

glycolate oxidase enzyme in maize. Maize is a C 4 plant 

and, thus, largely suppresses photorespiration by pumping 

CO2 into the vicinity of RubisCO ([Figure 3]). Unexpectedly, 

homozygous mutant plants were not capable of 

surviving in normal air and required CO2 enrichment for 

normal growth. Furthermore, glycolate accumulated in 

these plants and photosynthesis was suppressed by high 

oxygen concentrations. All these features are reminiscent 

of photorespiratory mutants in C3 plants [27]. The low 

rates of RubisCO oxygenase activity in C 4 plants seemingly 

produce enough phosphoglycolate to inhibit 

photosynthesis when accumulating. This often mentioned, 

but poorly studied toxic effect of phosphoglycolate 

and other photorespiratory metabolites on 

photosynthesis seems to be equally important for growth 

inhibition under conditions of high oxygenase activity as 

the loss of CO2 or NH4 + during later steps of the photorespiratory 

pathway. 

In the second study, photorespiratory mutants of the 

cyanobacterium Synechocystis were analysed [28 ]. Analogous 

to the situation in maize, oxygen fixation by 

RubisCO is also low in cyanobacteria because of an 

efficient CO2-concentrating mechanism. Moreover, at 

least some cyanobacteria are capable of excreting excess 

glycolate [29]. Despite of the low rates of phosphoglycolate 

synthesis, Synechocystis established three different 

routes for the metabolism of this compound (Figure 4): 

one pathway reminds of the metabolism that bacteria use 


Figure 3 

CCM in cyanobacteria, algae and higher plants. 

to grow on glycolate as a carbon source, the second 

resembles the photorespiratory pathway found in higher 

plants, and the third involves the complete oxidation of 

glycolate to CO2. Whereas mutants in single pathways 

were impaired in growth, only knock-out of all three pathways 

for glycolate conversion resulted in a conditional 

lethal phenotype. These data are important for two 

reasons: First, they suggest that the photorespiratory pathway 

might have evolved before the endosymbiosis of 

cyanobacteria forming the first photosynthetic eukaryotes. 

Second, a complete interruption of phosphoglycolate 

metabolism is probably lethal for all tested photosynthetic 

organisms under normal growth conditions independent of 

the amounts of phosphoglycolate formed. 

Manipulation of photorespiration and growth 

In theory, any reduction in photorespiration should 

enhance CO2 fixation and therefore growth. However, 


as discussed above, disruption of photorespiration causes 

strongly retarded growth of mutant plants. An alternative 

is the deviation of some of the phosphoglycolate formed 

by RubisCO into alternative pathways. Kebeish et al. [30] 

described the installation of the bacterial glycolate oxidation 

pathway in Arabidopsis chloroplasts that converts 

glycolate in three steps to glycerate and thus establishes a 

photorespiratory bypass. This pathway includes a CO 2 

release step analogous to the C2 pathway, but the authors 

provided evidence that shifting CO2 release from the 

mitochondrium to the chloroplast increased the CO 2 

concentration around RubisCO and as a result reduced 

RubisCO’s oxygenase activity in vivo. Moreover, energy 

and reducing equivalents may be saved in the bypass: it 

does not include release and refixation of ammonia and 

the energy from glycolate oxidation is saved in reducing 

equivalents and not burned by the formation of H 2O 2. 

Consequently, transgenic lines showed enhanced shoot 



Figure 4 

The multiple pathways for phosphoglycolate metabolism in 

Synechocystis. Phosphoglycolate is converted to glyoxylate in two 

enzymatic steps and then further metabolized to 3-phosphoglycerate (3- 

PGA) and/or CO 2 by three complementary pathways: blue: bacteria-like 

pathway; red: higher plant-like pathway; green: complete oxidation of 

glyoxylate to CO 2. 

and even root biomass production. It remains to be analysed 

which of the theoretical benefits of the bypass discussed 

are responsible for the enhanced growth phenotype. 

A clue to this question might come from an alternative 

approach where glycolate is completely oxidized to CO2 in 

the chloroplast using only two enzymatic steps (H Fahnenstich, 

PhD thesis, University of Cologne, 2008). This 

approach shares both the enrichment of CO2 in the chloroplast 

and the prevention of ammonia release with the 

photorespiratory bypass and because of this positive effects 

on growth are also evident [31]. Interestingly, both synthetic 

detours from photorespiration are reminiscent of the 

secondary photorespiratory pathways that naturally occur 

in Synechocystis [28 ]. It is of major interest to understand 

why these pathways have been lost from higher plants if 

synthetic re-engineering of the previous state was successful 

in augmenting photosynthetic capacity in Arabidopsis 

[30]. One reason might be the evolution of specific leaf 

architectures in individual species. For example, rice shows 

adaptations to maximize the scavenging of photorespired 

CO 2 and to enhance the diffusive conductance of CO 2 [32]. 

It is speculated that such an ultrastructure could minimize 

the benefits obtained from glycolate oxidation in the 

chloroplast in this species. 

Concluding remarks 

Recent studies added additional levels of complexity 

to the well-established photorespiratory pathway and 

support the view that photorespiration evolved in both, 

C 3 and C 4 plants, to prevent the accumulation of toxic 

levels of glycolate, which inevitably occurs if O2 is 

present. This together with the still limited knowledge 

on metabolite transport during photorespiration and 

the potential for biotechnological application will hopefully 

motivate significant future research efforts in this 

field. 

Acknowledgements 

We thank Andreas Weber for critical reading of the manuscript. This work 

was supported by the Deutsche Forschungsgemeinschaft grants MA2379/4- 

1 and 8-1 to VGM and PE819/4-1 to CP, both as part of the German 

Photorespiration Research Network Promics. 

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