Photorespiration
Hermann Bauwe, University of Rostock, Rostock, Germany
Based in part on the previous version of this Encyclopedia of Life Sciences
(ELS) article, Photorespiration by Thomas D Sharkey.
Photorespiration is the light-dependent release of carbon
dioxide initiated by ribulose-1,5-bisphosphate carbox-
ylase/oxygenase (Rubisco) in oxygen-producing photo-
synthetic organisms. It occurs because oxygen can
substitute for carbon dioxide in the first reaction of the
photosynthetic carbon dioxide-fixation process, causing
the idle synthesis of phosphoglycolate. Phosphoglycolate
is scavenged in the photorespiratory C2 cycle, which is an
essential auxiliary metabolic pathway that allows photo-
synthesis in oxygen-containing environments. Three out
of four misdirected carbon atoms are recovered and the
fourth is released as photorespiratory carbon dioxide.
Absolute rates vary in different organisms and they also
depend on environmental conditions, mainly oxygen,
carbon dioxide and temperature. They are highest in C3
plants and much reduced in other organisms, such as C4
plants, algae and cyanobacteria. In the presence of oxy-
gen, phosphoglycolate production is unavoidable and
cannot be eliminated.
Introduction
Photorespiration, in contrast to the light-independent
processes of day respiration and night respiration, is the
light-dependent release of carbon dioxide initiated by
ribulose 1,5-bisphosphate (RubP) carboxylase/oxygenase
(Rubisco) during oxygenic photosynthesis. It occurs
because oxygen can substitute for carbon dioxide in the
first reaction of the photosynthetic carbon dioxide-fixation
process, causing the idle synthesis of phosphoglycolate
(2PG). This toxic compound is recycled to 3-phosphogly-
cerate (3PGA) in the photorespiratory ‘C2 cycle’, which
ELS subject area: Plant Science
How to cite:
Bauwe, Hermann (February 2010) Photorespiration. In: Encyclopedia of
Life Sciences (ELS). John Wiley & Sons, Ltd: Chichester.
DOI: 10.1002/9780470015902.a0001292.pub2
ENCYCLOPEDIA OF LIFE SCIENCES & 2010, John Wiley & Sons, Ltd. www.els.net
Advanced article
Article Contents
. Introduction
. Photorespiratory C2 Cycle
. Photorespiratory Nitrogen Metabolism
. Metabolite Transport between Compartments
. Photorespiration and Photoinhibition
. Metabolic Engineering
. Origin and Evolution
Online posting date: 15th February 2010
recovers one molecule of 3PGA from two molecules of
2PG, sacrificing one carbon atom to photorespiratory
carbon dioxide (Husic et al., 1987). Functionally, the C2
cycle is an ancillary metabolic process that allows photo-
synthesis to occur in oxygen-containing environments.
Photorespiration is most evident in higher plants with
the C3 pathway of photosynthesis (C3 plants). Given that it
occurs concurrently with photosynthetic carbon dioxide
uptake, carbon dioxide release is normally concealed and
specific techniques are necessary for its measurement
(Sharkey, 1988). In C3 plants (i.e. most plants), the rates are
approximately 20% of the net-photosynthesis in moderate
conditions but can be higher in warmer and drier envi-
ronments (Cegelski and Schaefer, 2006; Long et al., 2006).
In the presence of unnaturally high concentrations of car-
bon dioxide, photorespiration is very low. Photo-
respiratory mutants die in normal air but grow healthily in
such artificial environments (Somerville, 2001). This is why
photorespiration is sometimes erroneously viewed as a
wasteful process without function. However, oxygenic
photosynthesis is only possible on the condition of
adequate photorespiratory metabolism and life on Earth
would look very different without it.
Photorespiratory C2 Cycle
In the presence of oxygen, photosynthesis is unavoidably
coupled to the synthesis of 2PG by Rubisco. The rate of this
process is essentially defined by the quantity and kinetic
properties of Rubisco in combination with the concen-
trations of ribulose-1,5-bisphosphate (RubP), oxygen and
carbon dioxide in its cellular environment. The reaction
starts with the enolization of RubP to a reactive 2,3-endiol
intermediate. Rubisco, in fact, evolved from a primordial
enolase (Ashida et al., 2005; Tabita et al., 2008). The endiol
reacts with carbon dioxide to form 3PGA but it can also
react with oxygen to produce 3PGA and 2PG, which is
itself an inhibitor of several important enzymes (Bowes
et al., 1971). Rubisco strongly favours carbon dioxide over
oxygen but it will inevitably also use oxygen whenever this
gas is present. Because the concentration of oxygen in the
atmosphere and in photosynthesising cells is very much
higher than that of carbon dioxide, the 2PG biosynthetic
1
 Photorespiration

Cytosol pIMDH
Chloroplast
ADP ATP
Malate OAA NADPH
GS2 NH+4
OAA Malate NADP+

Rubisco Gln Glu

Glycerate 3-phosphate RubP Glycolate 2-phosphate
GOGAT
O2 3PGA
Fdred Fdox
ADP 2OG
GLYK PGP Glu
ATP Pi
Malate
DiT1 DiT2 AMT
Glycolate Glycerate Malate

Peroxisome
Glycerate Glycerate Glycolate 2OG Glu NH+4
HPR2 pMDH
NADP+ Malate Malate NAD+ O2
HPR1 CAT GOX
NADPH OAA OAA NADH H2O H2O2

Hydroxypyruvate 0.5 O2 Glyoxylate

Ala Glu
SGT GGT
Pyr 2OG

SHMT Mitochondrion
Serine Glycine
THF GDC
CH2-THF
+
Malate OAA NADH NADH NAD NH3 CO
Complex 1 NAD(P)H DH 2
OAA Malate NAD+

Figure 1 The plant photorespiratory C2 cycle spans three organelles: the chloroplast, the peroxisome and the mitochondrion. The enzymes of the core
cycle are Rubisco, phosphoglycolate phosphatase (PGP), glycolate oxidase (GOX), serine-glyoxylate aminotransferase (SGT), glutamate-glyoxylate
aminotransferase (GGT), glycine decarboxylase (GDC), serine hydroxymethyltransferase (SHMT), peroxisomal hydroxypyruvate reductase (HPR1) and
glycerate kinase (GLYK). Catalase (CAT) detoxifies hydrogen peroxide. A cytosolic hydroxypyruvate reductase (HPR2) supports HPR1 when the peroxisomal
malate dehydrogenase (pMDH) does not provide NADH rapidly enough for hydroxypyruvate reduction. Photorespiratory ammonia is captured by glutamine
synthetase (GS2). The produced glutamine is then used by ferredoxin-dependent glutamate synthase (GOGAT) to recycle 2-oxoglutarate into fresh
glutamate for peroxisomal transamination.

rate can be very high. See also: Photosynthesis: The Calvin
Cycle; Rubisco
The C2 cycle converts the noxious 2PG into 3PGA.
Including Rubisco, it comprises a core of nine enzymatic
reactions and several essential ancillary enzymes. In plants,
these enzymes are distributed over four subcellular com-
partments: the chloroplast, the peroxisome, the mito-
chondrion and the cytosol (Figure 1). First, 2PG
phosphatase removes the phosphate. Glycolate then moves
out of the chloroplasts through poorly characterized gly-
colate/glycerate antiporter and diffuses into the peroxi-
somes via porin-like channels. In a first peroxisomal
reaction, the flavin mononucleotide-dependent enzyme
glycolate oxidase (GOX) oxidizes glycolate to glyoxylate,
consuming molecular oxygen and generating hydrogen
peroxide. The large amount of hydrogen peroxide gener-
ated is decomposed by the ancillary enzyme catalase, which
is part of a general scavenging network for reactive oxygen
species (Foyer et al., 2009). See also: Oxidative Stress and
Redox Signalling in Plants
Next, two peroxisomal aminotransferases work in par-
allel to convert glyoxylate to glycine. Glutamate-glyoxylate
aminotransferase uses glutamate as the amino donor.
The second enzyme, serine-glyoxylate aminotransferase,
performs two tasks in the C2 cycle simultaneously: trans-
amination of glyoxylate to glycine using serine as the amino
donor, and conversion of serine to hydroxypyruvate in the
opposed peroxisomal branch of the cycle.
Glycine moves into the mitochondria where the central
function of the C2 cycle takes place: conversion of the two-
carbon compound glycine (produced from 2PG) into the
three-carbon compound serine (to finally form 3PGA).
This requires two enzymes, glycine decarboxylase (GDC)
and serine hydroxymethyltransferase (SHMT). Both
enzymes are important for general one-carbon metabolism
in all cells (Hanson and Roje, 2001) but green leaf mito-
chondria contain extremely large amounts of GDC and
SHMT to cope with the high photorespiratory carbon flux
(Douce et al., 2001). They are highly susceptible to oxi-
dation (Taylor et al., 2004) and are likely targets for regu-
lation by thioredoxin (Marti et al., 2009).
GDC is a multienzyme system comprising three enzymes
(P-, T-, and L-protein) that successively react with a shared
substrate protein (H-protein). The entire process requires
one molecule each of glycine, tetrahydrofolate (THF)
and NAD+ to produce one molecule methylene tetra-
hydrofolate (CH2THF). In addition, one molecule each
of carbon dioxide and ammonia is released and NADH

2 ENCYCLOPEDIA OF LIFE SCIENCES & 2010, John Wiley & Sons, Ltd. www.els.net
 Photorespiration

produced. To rapidly provide GDC with fresh NAD+,
much of the generated NADH is recycled with-
in the mitochondria in a process that is largely uncoupled
from adenosine triphosphate (ATP) synthesis (Nunes-
Nesi et al., 2008). The remaining NADH is exported to
the cytosol via malate shuttles (Scheibe et al., 2005).
Because of this, photorespiratory metabolism has a
strong effect on the cellular NADH/NAD+ balance and
influences other cellular processes such as the tricarboxylic
acid cycle (Igamberdiev and Gardeström, 2003) and nitrate
assimilation (Dutilleul et al., 2005; Rachmilevitch et al.,
2004).
SHMT combines CH2THF with a second molecule
of glycine to make serine and regenerate THF for GDC.
It was found that SHMT also produces considerable
amounts of 5-formyl-THF (Figure 2). This compound
strongly inhibits SHMT and must be permanently detoxi-
fied (Collakova et al., 2008). See also: Folates
Serine goes back into the peroxisomes, where it delivers
its amino group to glyoxylate to produce glycine and
hydroxypyruvate, which becomes reduced to glycerate by
NADH-dependent hydroxypyruvate reductase (HPR1).
NADH cannot permeate the peroxisomal membrane and
must be provided by peroxisomal malate dehydrogenase
(pMDH), which oxidizes malate imported from the cyto-
sol. In contrast to the deleterious effect of blocks in other C2
cycle reactions, the deletion of neither HPR1 nor pMDH
strongly impairs plant growth (Cousins et al., 2008; Timm
et al., 2008). This is because hydroxypyruvate can exit the
peroxisome and alternatively be reduced to glycerate in
the cytosol by the auxiliary enzyme NADPH-dependent
hydroxypyruvate reductase (HPR2). Hydroxypyruvate
flux through the cytosol is small in moderate environments
and likely defined by the rate of NADH supply to HPR1. It
is speculated that the cooperation of peroxisomal and
cytosolic reactions allows more flexibility in the short-term
adaptation of photorespiratory metabolism to changing
environmental conditions (Timm et al., 2008).
In the chloroplasts, glycerate 3-kinase (GLYK) com-
pletes the photorespiratory C2 cycle by returning three of

CO2
10-Formyl-THF
5,10-Methylene-THF
H
Formate
O C O COOH
10 10
H N O CH2 N C
}
N CH
H E3 H
N CH2 C N CH2 H CH2
5 C C 5 C
HN
H CH2
C C C γCO
H2N N N H
n∼6
H }
E1 OH
E1 Glu

10
CH N
H 5,10-Methenyl-THF
N+ CH2
5 C

E2 SHMT

O H 10
C N 5-Formyl-THF
H
N+ CH2
5
C

Figure 2 Photorespiration is embedded into whole cell metabolism and manifold interactions with other metabolic pathways exist. For example, SHMT and
other enzymes are strongly inhibited by 5-formyl-THF, which is produced in considerable amounts by SHMT itself. Cellular metabolism would rapidly break
down if this noxious compound would not be detoxified and recycled to THF. This requires four folate-interconverting enzymes, 5,10-CH2THF
dehydrogenase combined with 5,10-methenyl-THF cyclohydrolase in a bifunctional enzyme (E1), 5-formyl-THF cycloligase (E2) and 10-formyl-THF
deformylase (E3). If E3 is blocked, plants accumulate massive amounts of glycine in normal air and need elevated carbon dioxide to survive (Collakova et al.,
2008).

ENCYCLOPEDIA OF LIFE SCIENCES & 2010, John Wiley & Sons, Ltd. www.els.net 3
 Photorespiration
four 2PG carbon atoms back to the Calvin cycle in the form
of 3PGA. GLYK is the only glycerate kinase that produces
3PGA. Most bacteria and animals do not use GLYK but a
glycerate 2-kinase, which produces 2PGA (Bartsch et al.,
2008; Boldt et al., 2005).
Photorespiratory Nitrogen
Metabolism
Half of the glycine flowing through the C2 cycle is decom-
posed to CH2THF, carbon dioxide and ammonia. C3 plants
recapture only approximately 50% of the carbon dioxide. In
contrast, photorespiratory ammonia is refixated with very
high efficiency. This requires two chloroplast-localized
enzymes, glutamine synthetase (GS) and glutamate synthase
(GOGAT), which together form the GS/GOGAT pathway.
First, GS binds ammonia to glutamate forming glutamine.
Next, GOGAT transfers the amido group from glutamine to
2-oxoglutarate (imported from the peroxisome) to yield
glutamate, which moves into the peroxisome to donate its
amino group to glyoxylate. GS was also detected in the
mitochondria, indicating that some photorespiratory
ammonia could be fixed within the mitochondria; however,
the physiological significance of this process is unproven
(Linka and Weber, 2005; Taira et al., 2004). The functioning
of this ‘photorespiratory nitrogen cycle’ (Keys et al., 1978) is
essential for photorespiratory metabolism (Coschigano
et al., 1998; Somerville, 2001). For example, the widely used
herbicide glufosinate inhibits GS and kills plants by
ammonia poisoning. Some crop plants have been made
glufosinate-resistant to allow selective weed control.
See also: Genetically Modified Plants
Metabolite Transport between
Compartments
Photorespiratory metabolism and nitrogen cycling both
require cooperation among three organelles. In addition,
reducing power must be provided by the chloroplasts and
mitochondria to the peroxisomes via the cytosol. All this
needs more than 10 distinct metabolite transmembrane
passages, but little is known about the participating
transport proteins and only few of them have been properly
identified (Reumann and Weber, 2006). See also: Plant
Chloroplasts and Other Plastids; Plant Mitochondria;
Plant Peroxisomes and Glyoxysomes
Photorespiration and Photoinhibition
Because photorespiration consumes ATP and reducing
power, it can be useful to the plant as an alternative electron
sink when carbon dioxide is not available or light intensity
is too high. This is not an essential function of photo-
respiration but it can gain some relevance when carbon
4 ENCYCLOPEDIA OF LIFE SCIENCES & 2010, John Wiley & Sons, Ltd. www.els.net
dioxide concentrations are close to the carbon dioxide
compensation point (where photosynthesis goes just fast
enough to fix the carbon dioxide released in photo-
respiration). This happens when plants have too little water
and the stomata on the leaves close, restricting water loss
but at the same time restricting carbon dioxide entry. From
a different perspective, it is known that photorespiratory
glycine contributes to the synthesis of the protective sub-
stance glutathione, which accumulates to high concen-
trations in the chloroplast stroma (Noctor et al., 1999). The
extent to which photorespiration contributes to the pro-
tection of plants against much light has been discussed
controversially (Brestic et al., 1995; Heber et al., 1996).
Under most conditions, plants use more efficient and flex-
ible mechanisms for the disposal of excess light energy
(Osmond et al., 1997). See also: Plant Light Stress
Metabolic Engineering
Photorespiratory metabolism allows photosynthesis but it
also inhibits photosynthesis: oxygen inhibits carbon di-
oxide fixation at Rubisco; oxygen fixation consumes RubP;
photorespiration releases carbon dioxide from previously
fixed carbon; photorespiration uses energy that could
otherwise be used for photosynthetic carbon reduction.
A reduction of these inhibitions is considered as desirable
but not easy to achieve. Reducing the capacity for
2PG metabolism evidently harms and even kills plants
(Blackwell et al., 1988; Kleczkowski, 1994; Somerville,
1986). Some hope lies in identifying better natural or
mutant Rubisco variants and integrating them into plants
(Andrews and Whitney, 2003). It is difficult to predict how
much this could improve photosynthesis because all
Rubiscos may be nearly perfectly adapted to the differing
carbon dioxide, oxygen and other conditions in their spe-
cific subcellular environments (Tcherkez et al., 2006).
Another strategy tries taking advantage of differences
between bacterial and plant glycolate metabolisms. For
example, in contrast to plant GOX, bacterial glycolate
dehydrogenases do not produce toxic hydrogen peroxide
and must not be contained in peroxisomes. Arabidopsis
plants engineered to harbour bacterial glycolate dehy-
drogenase, tartronic semialdehyde synthase and tartronic
semialdehyde reductase indeed grew better and produced
more biomass. It is thought that the artificially introduced
glycerate pathway, which converts glycolate into glycerate
and carbon dioxide directly within the chloroplasts,
favours carbon dioxide fixation by elevating the carbon
dioxide concentration in the vicinity of Rubisco (Kebeish
et al., 2007). If this strategy works in crop plants, it would
probably be an enormous achievement.
Origin and Evolution
The catalytic mechanism of Rubisco, which implies 2PG
synthesis in the presence of oxygen, evolved in strictly
 Photorespiration

anaerobic environments long before the invention of oxy-
genic photosynthesis (Tabita et al., 2008). The early evo-
lution of 2PG metabolism hence reflects the evolution of
oxygen-producing cyanobacteria between 3.8 and 2.5 bil-
lion years ago in the nearly anaerobic environment of the
Precambrian ocean.
Most extant cyanobacteria have highly efficient carbon-
concentrating mechanisms (CCM), which evolved
approximately 300 Ma, to rapidly capture inorganic car-
bon even at a very low concentration (Price et al., 2008).
CCMs strongly suppress 2PG synthesis, too, but cyano-
bacteria nevertheless require a functional photorespiratory
metabolism (Eisenhut et al., 2008). Cyanobacterial 2PG
recycling comprises two partially redundant pathways, a
C2 cycle very similar to that of plants and the bacterial
glycerate pathway (Figure 3).
Both pathways start by 2PG dephosphorylation and the
oxidation of glycolate to glyoxylate by glycolate dehy-
drogenase or a GOX-like oxidase. The glycerate pathway
circumvents the glycine-to-serine conversion by directly
converting glyoxylate into glycerate using tartronic acid
synthase and tartronic semialdehyde reductase. Only few
advanced cyanobacteria have a 3PGA-forming GLYK; all
others use 2PGA-forming glycerate kinases in combination
with phosphoglyceromutase for the generation of 3PGA.
Some cyanobacteria can also completely decompose
glyoxylate to carbon dioxide via oxalate decarboxylase and
formate dehydrogenase. If all three routes are artificially
inactivated, cyanobacteria accumulate glycolate and can
no longer survive in normal air. This shows that photo-
respiratory metabolism has been an essential partner of
oxygenic photosynthesis from the beginning. Approxi-
mately 1.2 billion years ago, cyanobacteria transferred this
capability via endosymbiosis to the evolutionary process,
leading to algae and plants (Rodriguez-Ezpeleta et al.,
2005). See also: Cyanobacteria; Photosynthesis and
Respiration in Cyanobacteria
Approximately 500 Ma, when land plants appeared on
the Earth, oxygen levels had increased from likely
approximately 2% at the time of the endosymbiotic event

Rubisco
Glycerate 3-phosphate RubP Glycolate 2-phosphate
CO2
O2 3PGA NADH

Decarboxylation pathway
PGM FDH
NAD+

Glycerate 2-phosphate PGP Formate

ADP ADP Pi
GLYK GK CO2
ODC
ATP ATP +
Glyc
NAD erat
e pa
NADH thw
Glycerate ay Glycolate Oxalate

NAD+ TSR Tartronic CO2 NAD+ H2O2

HPR semialdehyde GLCDH GXO
NADH NADH O2

Hydroxypyruvate TSS Glyoxylate

Glu
SGT GGT
2OG

SHMT
Serine Glycine
THF GDC
CH2-THF
+
NADH NAD NH3 CO2

Figure 3 Cyanobacteria recycle phosphoglycolate via two partially redundant pathways, a plant-like C2 cycle (metabolites in blue, enzymes in red) and the
bacterial glycerate pathway (black route). Both pathways start with phosphoglycolate phosphatase (PGP) and glycolate dehydrogenase (GLCDH). The
glycerate pathway circumvents the glycine-to-serine conversion by directly converting glyoxylate into glycerate using tartronic semialdehyde synthase (TSS)
and tartronic semialdehyde reductase (TSR). Enzymes of the plant-like branch are serine-glyoxylate aminotransferase (SGT), glutamate-glyoxylate
aminotransferase (GGT), glycine decarboxylase (GDC), serine hydroxymethyltransferase (SHMT) and hydroxypyruvate reductase (HPR). Only few advanced
cyanobacteria have a plant-type 3PGA-forming glycerate kinase (GLYK, green route); all others use 2PGA-forming glycerate kinases (GK) in combination with
phosphoglyceromutase (PGM) for the generation of 3PGA. Some cyanobacteria can also completely decompose glyoxylate to carbon dioxide (grey route)
via oxalate decarboxylase (ODC) and formate dehydrogenase (FDH). Cyanobacterial mutants without functioning phosphoglycolate metabolism cannot
survive in normal environments (Eisenhut et al., 2008).

ENCYCLOPEDIA OF LIFE SCIENCES & 2010, John Wiley & Sons, Ltd. www.els.net 5
 Photorespiration
to approximately the levels we have today, but carbon
dioxide was still 15-fold higher than in our present
atmosphere. Massive photosynthetic activity in the Carbo-
niferous period (360–300 Ma) then resulted in an inter-
mittent drop in carbon dioxide levels and a rise in oxygen
levels (Berner, 2006). See also: Earth: Changes Through
Time
During the past 25 million years, carbon dioxide levels
were generally low (Kürschner et al., 2008). Temperature
was another important factor in some areas because the
specificity of Rubisco for carbon dioxide over oxygen is
worse at high temperatures and the solubility of oxygen
declines more slowly than that of carbon dioxide. Adapting
to lower carbon dioxide levels and higher temperatures, a
number of land plants independently evolved CCMs that
are known as C4 photosynthesis. This pathway is based on
a prefixation of carbon dioxide in the mesophyll by phos-
phoenolpyruvate carboxylase to first make a four-carbon
(C4) compound. The enzyme efficiently captures carbon
dioxide even at a very low concentration, creating a large
gradient in carbon dioxide concentration between the
inside of the leaf and the outside environment. The C4
compound then moves to the Rubisco-containing bundle
sheath cells, where the carbon dioxide is released by a C4
acid decarboxylase. Through this mechanism, Rubisco
operates at greatly elevated carbon dioxide levels and 2PG
synthesis is low though not entirely absent. 2PG synthesis is
evident, for example, because GOX-deficient maize thrives
only in carbon dioxide-enriched air but not in a normal
environment (Zelitch et al., 2009). Despite these advan-
tages, C4 photosynthesis is not competitive in all climates
and far most land plants use the C3 photosynthetic path-
way. See also: Kranz Anatomy and the C4 Pathway; Plant
Temperature Stress
Paradoxically, photorespiration not only provided
pressure towards the evolution of C4 photosynthesis but
also triggered this process by inventing a first though not
very efficient CCM. This appears likely at least from the
analysis of C3 –C4 intermediate plants. These predecessors
of C4 plants produce glycine in all photosynthetic cells but,
due to a restriction of GDC to the bundle sheath, glycine is
decarboxylated only in these specific vein-surrounding cells
(Rawsthorne, 1992). It is quite possible that this favoured
the subsequent accumulation of chloroplasts in the bundle
sheath and prepared the path for C4 plant evolution
(Bauwe, 2010).
During the past 50 years, global carbon dioxide con-
centration has increased by approximately 20%. This has
probably decreased photorespiration worldwide and, as
the carbon dioxide concentration continues to increase in
the future, photorespiration will continue to fall. The
higher efficiency of C3 plants under these conditions could
affect competition between C3 and C4 plants and alter
species composition and diversity in many ecosystems.
Some researchers believe that higher atmospheric carbon
dioxide levels will increase crop yields; however, glo-
bal climate is difficult to predict and local changes to
temperature, rainfall and other determinant factors for
6 ENCYCLOPEDIA OF LIFE SCIENCES & 2010, John Wiley & Sons, Ltd. www.els.net
agricultural productivity could more than offset any
productivity gains. See also: Climate Change and Biogeo-
chemical Impacts
References
Andrews TJ and Whitney SM (2003) Manipulating ribulose
bisphosphate carboxylase/oxygenase in the chloroplasts of
higher plants. Archives of Biochemistry and Biophysics 414:
159–169.
Ashida H, Danchin A and Yokota A (2005) Was photosynthetic
RuBisCO recruited by acquisitive evolution from RuBisCO-
like proteins involved in sulfur metabolism? Research in
Microbiology 156: 611–618.
Bartsch O, Hagemann M and Bauwe H (2008) Only plant-type
(GLYK) glycerate kinases produce D-glycerate 3-phosphate.
FEBS Letters 582: 3025–3028.
Bauwe H (2010) Photorespiration – the bridge to C4 photo-
synthesis. In: Raghavendra AS and Sage R (eds) C4 Photo-
synthesis and Related CO2 Concentrating Mechanisms. New
York: Springer.
Berner RA (2006) GEOCARBSULF: a combined model for
Phanerozoic atmospheric O2 and CO2. Geochimica et Cosmo-
chimica Acta 70: 5653–5664.
Blackwell RD, Murray AJS, Lea PJ et al. (1988) The value of
mutants unable to carry out photorespiration. Photosynthesis
Research 16: 155–176.
Boldt R, Edner C, Kolukisaoglu Ü et al. (2005) D-glycerate 3-
kinase, the last unknown enzyme in the photorespiratory cycle
in Arabidopsis, belongs to a novel kinase family. Plant Cell 17:
2413–2420.
Bowes G, Ogren WL and Hageman RH (1971) Phosphoglycolate
production catalysed by ribulose diphosphate carboxylase.
Biochemical and Biophysical Research Communications 45:
716–722.
Brestic M, Cornic G, Fryer MJ et al. (1995) Does photorespiration
protect the photosynthetic apparatus in french bean leaves from
photoinhibition during drought stress. Planta 196: 450–457.
Cegelski L and Schaefer J (2006) NMR determination of photo-
respiration in intact leaves using in vivo 13CO2 labeling. Journal
of Magnetic Resonance 178: 1–10.
Collakova E, Goyer A, Naponelli V et al. (2008) Arabidopsis 10-
formyl tetrahydrofolate deformylases are essential for photo-
respiration. Plant Cell 20: 1818–1832.
Coschigano KT, Melo-Oliveira R, Lim J et al. (1998) Arabidopsis
gls mutants and distinct Fd-GOGAT genes: implications for
photorespiration and primary nitrogen assimilation. Plant Cell
10: 741–752.
Cousins AB, Pracharoenwattana I, Zhou W et al. (2008) Perox-
isomal malate dehydrogenase is not essential for photo-
respiration in Arabidopsis but its absence causes an increase in
the stoichiometry of photorespiratory CO2 release. Plant Phy-
siology 148: 786–795.
Douce R, Bourguignon J, Neuburger M et al. (2001) The glycine
decarboxylase system: a fascinating complex. Trends in Plant
Science 6: 167–176.
Dutilleul C, Lelarge C, Prioul JL et al. (2005) Mitochondria-
driven changes in leaf NAD status exert a crucial influence on
the control of nitrate assimilation and the integration of carbon
and nitrogen metabolism. Plant Physiology 139: 64–78.

Eisenhut M, Ruth W, Haimovich M et al. (2008) The photo-
respiratory glycolate metabolism is essential for cyanobacteria
and might have been conveyed endosymbiontically to plants.
Proceedings of the National Academy of Sciences of the USA
105: 17199–17204.
Foyer CH, Bloom AJ, Queval G et al. (2009) Photorespiratory
metabolism: genes, mutants, energetics, and redox signaling.
Annual Review of Plant Biology 60: 455.
Hanson AD and Roje S (2001) One-carbon metabolism in higher
plants. Annual Review of Plant Physiology and Plant Molecular
Biology 52: 119–137.
Heber U, Bligny R, Streb P et al. (1996) Photorespiration is
essential for the protection of the photosynthetic apparatus of
C3 plants against photoinactivation under sunlight. Botanica
Acta 109: 307–315.
Husic DW, Husic HD and Tolbert NE (1987) The oxidative
photosynthetic carbon cycle or C2 cycle. Critical Reviews in
Plant Sciences 5: 45–100.
Igamberdiev AU and Gardeström P (2003) Regulation of NAD-
and NADP-dependent isocitrate dehydrogenases by reduction
levels of pyridine nucleotides in mitochondria and cytosol of
pea leaves. Biochimica et Biophysica Acta 1606: 117–125.
Kebeish R, Niessen M, Thiruveedhi K et al. (2007) Chloroplastic
photorespiratory bypass increases photosynthesis and biomass
production in Arabidopsis thaliana. Nature Biotechnology 25:
593–599.
Keys AJ, Bird IF, Cornelius MJ et al. (1978) Photorespiratory
nitrogen cycle. Nature 275: 741–743.
Kleczkowski LA (1994) Inhibitors of photosynthetic enzymes/
carriers and metabolism. Annual Review of Plant Physiology 45:
339–367.
Kürschner WM, Kvacek Z and Dilcher DL (2008) The impact of
Miocene atmospheric carbon dioxide fluctuations on climate
and the evolution of terrestrial ecosystems. Proceedings of the
National Academy of Sciences of the USA 105: 449–453.
Linka M and Weber APM (2005) Shuffling ammonia between
mitochondria and plastids during photorespiration. Trends in
Plant Science 10: 461–465.
Long SP, Zhu XG, Naidu SL et al. (2006) Can improvement in
photosynthesis increase crop yields? Plant, Cell and Environ-
ment 29: 315–330.
Marti MC, Olmos E, Calvete JJ et al. (2009) Mitochondrial and
nuclear localization of a novel pea thioredoxin: identification
of its mitochondrial target proteins. Plant Physiology 150:
646–657.
Noctor G, Arisi AM, Jouanin L et al. (1999) Photorespiratory
glycine enhances glutathione accumulation in both the chlor-
oplastic and cytosolic compartments. Journal of Experimental
Botany 50: 1157–1167.
Nunes-Nesi A, Sulpice R, Gibon Y et al. (2008) The enigmatic
contribution of mitochondrial function in photosynthesis.
Journal of Experimental Botany 59: 1675–1684.
Osmond CB, Badger M, Maxwell K et al. (1997) Too many
photons: photorespiration, photoinhibition and photooxida-
tion. Trends in Plant Science 2: 119–121.
Price GD, Badger MR, Woodger FJ et al. (2008) Advances in
understanding the cyanobacterial CO2-concentrating-mech-
anism (CCM): functional components, Ci transporters, diver-
sity, genetic regulation and prospects for engineering into
plants. Journal of Experimental Botany 59: 1441–1461.
ENCYCLOPEDIA OF LIFE SCIENCES & 2010, John Wiley & Sons, Ltd. www.els.net
Photorespiration
Rachmilevitch S, Cousins AB and Bloom AJ (2004) Nitrate
assimilation in plant shoots depends on photorespiration.
Proceedings of the National Academy of Sciences of the USA
101: 11506–11510.
Rawsthorne S (1992) C3-C4 intermediate photosynthesis – linking
physiology to gene expression. Plant Journal 2: 267–274.
Reumann S and Weber AP (2006) Plant peroxisomes respire in the
light: some gaps of the photorespiratory C2 cycle have become
filled – others remain. Biochimica et Biophysica Acta 1763:
1496–1510.
Rodriguez-Ezpeleta N, Brinkmann H, Burey SC et al. (2005)
Monophyly of primary photosynthetic eukaryotes: green
plants, red algae, and glaucophytes. Current Biology 15:
1325–1330.
Scheibe R, Backhausen JE, Emmerlich V et al. (2005) Strategies
to maintain redox homeostasis during photosynthesis under
changing conditions. Journal of Experimental Botany 56:
1481–1489.
Sharkey TD (1988) Estimating the rate of photorespiration in
leaves. Physiologia Plantarum 73: 147–152.
Somerville CR (1986) Analysis of photosynthesis with mutants of
higher plants and algae. Annual Review of Plant Physiology 37:
467–506.
Somerville CR (2001) An early Arabidopsis demonstration
resolving a few issues concerning photorespiration. Plant Phy-
siology 125: 20–24.
Tabita FR, Satagopan S, Hanson TE et al. (2008) Distinct form I,
II, III, and IV Rubisco proteins from the three kingdoms of life
provide clues about Rubisco evolution and structure/function
relationships. Journal of Experimental Botany 59: 1515–1524.
Taira M, Valtersson U, Burkhardt B et al. (2004) Arabidopsis
thaliana GLN2-encoded glutamine synthetase is dual targeted
to leaf mitochondria and chloroplasts. Plant Cell 16:
2048–2058.
Taylor NL, Day DA and Millar AH (2004) Targets of stress-
induced oxidative damage in plant mitochondria and their
impact on cell carbon/nitrogen metabolism. Journal of
Experimental Botany 55: 1–10.
Tcherkez GGB, Farquhar GD and Andrews TJ (2006) Despite
slow catalysis and confused substrate specificity, all ribulose
bisphosphate carboxylases may be nearly perfectly optimized.
Proceedings of the National Academy of Sciences of the USA
103: 7246–7251.
Timm S, Nunes-Nesi A, Pärnik T et al. (2008) A cytosolic pathway
for the conversion of hydroxypyruvate to glycerate during
photorespiration in Arabidopsis. Plant Cell 20: 2848–2859.
Zelitch I, Schultes NP, Peterson RB et al. (2009) High glycolate
oxidase activity is required for survival of maize in normal air.
Plant Physiology 149: 195–204.
Further Reading
Allen JF and Martin W (2007) Evolutionary biology: out of thin
air. Nature 445: 610–612.
Andrews TJ and Lorimer GH (1978) Photorespiration – still
unavoidable? FEBS Letters 90: 1–9.
Canfield DE (2005) The early history of atmospheric oxygen:
homage to Robert M. Garrels. Annual Review of Earth and
Planetary Sciences 33: 1–36.
7
 Photorespiration

Giordano M, Beardall J and Raven JA (2005) CO2 concentrating
mechanisms in algae: mechanisms, environmental modulation,
and evolution. Annual Review of Plant Biology 56: 99–131.
Gould SB, Waller RF and McFadden GI (2008) Plastid evolution.
Annual Review of Plant Biology 59: 491–517.
Hetherington AM and Raven JA (2005) The biology of carbon
dioxide. Current Biology 15: R406–R410.
Schwartzman D, Caldeira K and Pavlov A (2008) Cyanobacterial
emergence at 2.8 Gya and greenhouse feedbacks. Astrobiology
8: 187–203.
Tolbert NE (1997) The C2 oxidative photosynthetic carbon cycle.
Annual Review of Plant Physiology and Plant Molecular Biology
48: 1–25.

8 ENCYCLOPEDIA OF LIFE SCIENCES & 2010, John Wiley & Sons, Ltd. www.els.net