Ino ganic Polyphospha e in he Mic obial Wo ld. Eme ging Roles o a Mul i ace ed Biopolyme
Tomás Albi and Au elio Se ano*
Ins i u o de Bioquímica Vege al y Fo osín esis, Cen o de In es igaciones Cien í icas Isla Ca uja, CSIC y
Uni e sidad de Se illa, A . Amé ico Vespucio 49, 41092 Se illa, SPAIN
*To whom co espondence should be add essed: D . Au elio Se ano, Ins i u e o Plan Biochemis y and
Pho osyn hesis, CSIC and Uni e si y o Se ille, A . Amé ico Vespucio 49, 41092 Se ille, SPAIN. Phone: ++
34 95 4489524. Fax: ++ 34 95 4460165. E-mail: au elio@ib .csic.es. Web:
h p://www.ib .csic.es/en/bioene ge ics-phospha e
ABSTRACT
Ino ganic polyphospha es (polyP) a e linea polyme s o ens o hund eds o hophospha e esidues linked by
phosphoanhyd ide bonds. These ai ly abundan biopolyme s occu in all ex an o ms o li e, om
p oka yo es o mammals, and could ha e played a ele an ole in p ebio ic e olu ion. Since he i s
iden i ica ion o polyP deposi s as me ach oma ic o olu in g anules in yeas s in he 19 h cen u y, an
inc easing numbe o a ied physiological unc ions ha e been epo ed. Due o hei “high ene gy” bonds
analogous o hose in ATP and hei p ope ies as polyanions, polyP se e as mic obial phosphagens o a
a ie y o biochemical eac ions, as a bu e agains alkalis, as a s o age o Ca2+ and as a me al-chela ing
agen . In addi ion, ecen s udies ha e e ealed polyP impo ance in signaling and egula o y p ocesses, cell
iabili y and p oli e a ion, pa hogen i ulence, as a s uc u al componen and chemical chape one, and as
modula o o mic obial s ess esponse. This e iew summa izes he cu en s a us o knowledge and u u e
pe spec i es o polyP unc ions and hei ela ed enzymes in he mic obial wo ld.
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KEYWORDS
Ino ganic polyphospha e; Ca ion chela o ; Nu ien de iciency; S ess P o ec ion; Cell signaling; Chemical
chape one.
ACKNOWLEDGMENTS
The au ho s a e hank ul o all esea che s whose pape s ha e been used o his e iew, as well as o hose
o he s ha we e no ci ed because o limi ed space. Pa o his wo k was suppo ed by esea ch g an s om
he Spanish (BFU2004-00843, BFU2007-61887, BFU2010-15622) and Andalusian Regional (PAIDI g oup
BIO-261) Go e nmen s, all o hem pa ially unded by he EU FEDER p og am. PAIDI g oup BIO-261
belongs o he CeiA3 and AndaluciaTECH Uni e si y Campuses o In e na ional Excellence. Au ho s hank
D . M. R. Gómez-Ga cía o help ul sugges ions and discussions.
PolyP Chemis y and Biochemis y. Enzymes In ol ed in PolyP Syn hesis and Deg ada ion.
1. S uc u e and Chemical Composi ion
Ino ganic polyphospha es, polyP, a e polyme s o o hophospha e (Pi) esidues linked by phosphoanhyd ide
P-O-P bonds . They a e o en e med as “condensed phospha es” since hey a e composed by se e al Pi uni s
( om h ee up o housands) connec ed by oxygen b idges. Con a y o long-chained polyP, which a e poo ly
soluble in wa e , he majo i y o polyP a e s able in neu al aqueous solu ions e en a high empe a u es.
Conside ing hei chemical s uc u e (Kulae e al. 2005) polyP a e di ided in o h ee classes: cyclic
condensed phospha es (also e e ed as me aphospha es, PnO3nn-, whose simples membe is cyclic-
iphospha e), linea polyphospha es (o linea me aphospha es, PnO3n+1 (n+2)-, whose sho es componen is
ipolyphospha e), and las ly, he “ul aphospha es” o b anched polyphospha es (Fig.1).
PolyP is pe haps one o he biopolyme s wi h he highes densi y o nega i e cha ge. I s analogous s uc u e o
he RNA and o he polyanions leads o compa able eac i i y. Fo ins ance, bo h polyme s inc ease
luo escence o DAPI, which can po en ially p o oke misin e p e a ions. As a esul , he de elopmen o new
polyP speci ic sensi i e and selec i e de ec ion echniques, and i s applica ion was c i ical o u he p og ess
on polyP esea ch (Angelo a e al. 2014). In ac , in spi e o hei disco e y in he end o he 19 h cen u y
(Babes 1895) and hei wide occu ence, polyP was la gely dismissed as a “molecula ossil” (Ko nbe g
1999). Fo una ely, hese ecen s udies ha e e ealed he eal physiological impo ance o polyP, s a ing an
eme ging in e es in polyP esea ch.
2. Na u al Occu ence o PolyP
Polyphospha e is ubiqui ous in li ing beings ha ing being ound in a chaea, bac e ia, algae, ungi, p o is s,
plan s, insec s and mammals (B own and Ko nbe g 2004; Docampo e al. 2005a; Rao e al. 2009). PolyP
ese es we e o mely disco e ed in bac e ia and unicellyla euka yo es being denno ed as me ach oma ic o
olu in g anules due o hei me ach oma ic e ec - hey appea ed when s ained wi h me hylene blue. La e ,
once polyP was p o en as one o i s main componen s, hey we e also e e ed as polyphospha e g anules o
acidocalcisomes (Docampo e al. 2005a). Besides his widely dis ibu ion among li ing o ganisms, he
amoun and chemical s uc u e o polyP ese es may a y depending he species and he pa icula g ow h
condi ions. In gene al, p oka yo es and p o is s a e able o accumula e polyP a highe a es han mul icellula
euka yo es.
3. Enzymes In ol ed in PolyP Syn hesis
Syn hesis o PolyP in P oka yo ic Mic oo ganisms: Polyphospha e Kinase
Mos s udies conce ning p o eins in ol ed in polyP biosyn hesis ha e been ocused on mic oo ganisms,
namely bac e ia, including pa hogenic and phospha e-accumula ing s ains, yeas s and pa asi ic p o is s.
Based on hese indings, some o hologs ha e been iden i ied in mic oo ganisms o o he axonomic g oups.
Ne e heless, o da e he e a e s ill nume ous o ganisms wi h no a che ypical o hologs iden i ed so a , in
spi e o being able o accumula e high polyP le els. Consequen ly, i is deduced ha hey should ha e
al e na i e pa hways o polyP syn hesis.
In p oka yo es -and in some mic obial euka yo es as well (Zhang e al. 2007)- polyP is mainly sin hesized by
polyphospha e kinase 1 (PPK1; polyphospha e:ADP phospho ans e ase, EC 2.7.4.1), which ca alyzes he
e e sible ans e o he ene gy- ich γ-phospha e om ATP o enlonga e he polyP chain.
PolyPn + ATP ↔ PolyPn+1 + ADP
PPK1 (P am PF02503) is a membe o he phospho ans e ases supe amily, and exhibi s o he enzyma ic
ac i i ies including ATP syn hesis om polyP, nucleoside-diphospha e kinase, guanosine 5′- e aphospha e
syn hesis and au ophospho yla ion (Tzeng and Ko nbe g 2000). A genomes sc eening using he BLAST
engine e ealed ppk1 homologs in mo e han 354 p oka yo es (Tzeng and Ko nbe g 1998). Howe e , no ppk1
homologs ha e been iden i ied so a in highe euka yo es, bo h highe plan s and animals. Mo eo e , a ious
s udies ha e p o ed he impo ance o ppk1, and PPK1 has been shown o be an essen ial enzyme. Lack o
PPK1 se e ely comp omised cell iabili y o many bac e ia unde s a iona y-g ow h phase and hei e ec i e
esponses o a wide ange o s ess ac o s, such as hea , UV ligh , pH, an ibio ics, e c. Simila ly, bac e ial
mu an s lacking PPK1 a e de ec i e in cell mo ili y, quo um sensing, bio ilm o ma ion and i ulence, and
show ul as uc u al de ec s (B own and Ko nbe g 2008; F aley e al. 2007; Rashid e al. 2000b; Sanyal e al.
2013). As a esul , ppk1 has been p oposed as a no el a ge o nex gene a ion an ibio ics.
None heless, PPK1 is no he sole enzyme esponsible o polyP syn hesis. In pa icula , high Mm polyP we e
iden i ied in ppk1-lacking null mu an s o Pseudomonas ae uginosa (Ishige e al. 2002). The al e na i e
enzyme was called PPK2 (P am PF03976). Simila ly o ppk1, ppk2 is absen in plan s and me azoans and has
been claimed o ha e a ole in i ulence o bac e ial pa hogens, in connec ion wi h algina e syn hesis and
bio ilm o ma ion, being hen conside ed as an a ac i e a ge o an ibio ics. Howe e , PPK2 is equen ly a
polyP-deg ading enzyme since i s capaci y o use polyP o GTP syn hesis is 75- old g ea e han i s Poly P
syn he ic ac i i y om GTP (Ishige e al. 2002). PPK2 can also se e as a PolyP:AMP phospho ans e ase
(EC 2.7.4.B2) and PolyP:ADP phospho ans e ase (Ishige and Noguchi 2000):
PolyPn + AMP ↔ PolyPn-1 + ADP
Con e sely o PPK1, PPK2 is no s ic ly speci ic o ATP and i is able o e icien ly use ei he GTP o ATP.
Many mic obial genomes encode mul iple ppk2 pa alogs (Zhang e al. 2002). In ac , he e a e p obably h ee
sub amilies o PPK2 enzymes con aining a single o wo homologous PPK2 domains. Thus, whe eas class I
PPK2 is monodomain and ca alyzes NTP syn hesis om NDP, classes II and III a e bi-domain PPK2 enzymes
which ca alyse he syn hesis o NMP, o bo h NMP and NDP, espec i ely (Mo omu a e al. 2014). Likewise
ppk1, ppk2 widely occu among p oka yo ic mic oo ganisms, and hund eds o ppk2 homologs ha e been
iden i ied o da e. Howe e , many bac e ia should syn hesize polyP by unknown enzymes, since one- hi d o
bac e ial species known so a lack bo h ppk1 and ppk2 (Whi ehead e al. 2014).
Syn hesis o PolyP in P o is s: A p and VTC P o eins
In he slime mold Dic yos ellium discoideum a new ype o PPK, named DdPPK2, was iden i ied. This
enzyme is a complex o h ee ac in- ela ed p o eins (A p), which can polyme ize in o an ac in-like ilamen
concu en ly wi h he e e sible syn hesis o polyP chain om ATP (Gomez-Ga cia and Ko nbe g 2004;
Spudich 2004).
In yeas and ypanosomes (Lande e al. 2013) an al e na i e pa hway esponsible o polyP syn hesis ha
in ol es VTC4, a subuni o he acuola anspo chape one (VTC) complex, has been desc ibed. VTC4 is a
membe o he Conse ed P o ein Domain amily VTC (P am PF09359), which belongs o he CYTH-like
phospha ases supe amily (cl11964). S. ce e isiae VTC complex is also in ol ed in se e al o he cellula

p ocesses, like acuola -memb ane usion (Ho ho n e al. 2009; Ogawa e al. 2000a; U enweile e al. 2007),
mic oau ophagy (Cohen e al. 1999; Ho ho n e al. 2009; Mulle e al. 2002; Ogawa e al. 2000a; U enweile
e al. 2007). Homologs o VTC4 ha e been in e ed in he genomes o apicomplexan p o is s, ungi and
mic oalgae (Aksoy e al. 2014). Chlamydomonas einha d ii VTC1 is equi ed o polyP syn hesis and polyP
g anule accumula ion in acidocalcisomes. A de icien acidocalcisome o ma ion in p o is an cells dep i ed o
N, P, o mainly S, may impac a ious unc ion associa ed wi h ene ge ics, a icking o pe iplasmic p o eins
and egula ion o cellula p ocesses (Aksoy e al. 2014; Mo eno and Docampo 2013).
O he Enzymes o PolyP Syn hesis
The dolichyl diphospha e:polyphospha e phospho ans e ase (EC 2.7.4.20) was ela ed o he syn hesis o he
small ac ion o polyP associa ed wi h he acuola memb ane o Saccha omyces ce e isiae (Schombu g and
S ephan 1997), and pe o ms he ollowing eac ion:
Dolichyl diphospha e + PolyPn → Dolichyl phospha e + PolyPn-1
Las ly, an 3-phospho-D-glyce ol-phospha e:polyphospha e phospho ans e ase (EC 2.7.4.17) was ound in he
ungus Neu ospo a c assa (Kukae e al. 1971). The enzyme, which has no been pu i ied and needs u he
in es iga ions, ca alyzes he ollowing eac ion:
3-Phospho-D-glyce ol-1-phospha e + PolyPn → 3-Phosphoglyce a e + PolyPn+1
4. Enzymes ha Deg ade PolyP
Exopolyphospha ase and Guanosine Pen aphospha e Hyd olase
The main enzyme esponsible o polyP usage in mic oo ganisms is he exopolyphospha ase (PPX;
Polyphospha e phosphohyd olase, EC 3.6.1.11). PPX hyd olyzes and p ocessi ely spli s Pi om he end o
he polyP chain:
PolyPn + H2O → PolyPn-1 + Pi
Two majo non-homologous classes o PPX a e de ined based on hei p ima y s uc u e. A i s PPX class is
es ablished by he a che ypical exopolyphospha ase PPX1, i s iden i ied in Saccha omyces ce e isiae, and
hei o hologues la e desc ibed in yeas s, o he ungi and p o is s. PPX1 belongs o he supe amily o DHH-
DHHA2 phosphoes e ases (P am PF02833), which also includes he p oka yo ic amily II py ophospha ases
(Young e al. 1998) and he Nudix hyd olase amily (Lone i e al. 2011). Some o hese Nudix p o eins, such
as he human p o ein h-p une, a binding p o ein o he me as asis supp esso nm23-H1, ha e been p o ed o
e icien ly hyd olyze polyP (Tammenkoski e al. 2008). The human p o ein h-p une and he yeas PPX1
p o eins sha e a high sequence iden i y (27%). PPX1 is an ex emely ac i e phoshohyd olase which can
hyd olyze polyP, adenosine e aphospha e and GPT; bu does no hyd olyze PPi o NTPs.
A second exopolyphospha ase class includes he Ppx-GppA polyphospha ases (P am PF02541) which belong
o he suga kinase/ac in/hsp 70 supe amily. Ppx-GppA exopolyphospha ases a e widely dis ibu ed among
bac e ia and a chaea, p ocessi ely hyd olyse linea polyP o 3 up o housands o Pi esidues, and also ha e
nucleoside iphospha ase (NTPase) ac i i y (Albi and Se ano 2014). Thus, p oka yo ic PPXs and euka yo ic
( ungal/p o is an) PPXs belong o di e en amilies o polyphospha ases and do no ha e s uc u al simila i y.
In addi ion, bac e ia posses ano he Ppx-GppA exopolyphospha ase sha ing ca 40% sequence simila i y wi h
i s a che ypical p oka yo ic pa alog and ca aly ically less e icien han he la e , he guanosine
pen aphospha e phosphohyd olase (GppA, EC 3.6.1.40) which also ca alyzes he ollowing eac ion:
Guanosine 5’- iphospha e, 3’-diphospha e → Guanosine 5’-diphospha e,3’-diphospha e + Pi
Endopolyphospha ase
Besides PPX1 exopolyphospha ase, yeas s, ungi and p o is s also posses an endopolyphospha ase enzyme.
The a che ypical endopolyphospha ase o S. ce e isiae (PPN1; Polyphospha e depolyme ase, EC 3.6.1.10) is
a ansmemb ane bi opic p o ein which belong o he Calcineu in-like phosphoes e ase supe amily (P am
PF00149), and clea es long polyP in o sho e polyP molecules wi hou eleasing Pi (Se hu aman e al. 2001):
PolyPn + H2O → oligopolyphospha es
In ich g ow h condi ions, yeas PPN1 ac s as an endopolyphospha ase in he p esence o Mg2+. Howe e ,
unde ce ain s ess condi ions, such as oxic hea y-me als, PPN1 shi s o an Co2+-dependen
exopolyphospha ase ac i i y (And ee a e al. 2015).
Func ions o PolyP in Mic oo ganisms
1. PolyP as a S uc u al Componen
One o he mos exci ing chemical ea u es o polyP is i s s ong abili y o in e ac wi h a a ie y o ino ganic
and o ganic compounds esul ing in e na y complexes. Thus, polyP (wi h and a e age leng h o 150 Pi
esidues) can o m complexes wi h poly-β-hyd oxybu y a e (mean size o 170) an Ca2+ ions. In he p oposed
s uc u e, poly-β-hyd oxybu y a e (PHB) co esponds o he ou e laye which is di ec ly in con ac wi h he
lipid memb ane. Inside, PHB es e g oups a e bonded o polyP by ionic in e ac ions and o Ca2+ by ion dipoles
(Reusch and Sado 1988). The polyP/Ca2+/PHB complex has been de ec ed in he plasma memb ane o many
na u ally compe en bac e ia, and in a ious subcellula compa men s o euka yo es (Reusch 1989). This
e na y complex cons i u es a ansien channel inc easing memb ane pe meabili y - selec i e o Ca2+ ions -
which p obably plays an impo an physiological ole in compe ence o DNA en y and ans o ma ion
(Cas uma e al. 1995).
Fu he esea ches in mammals suppo his assump ion (Dedko a and Bla e 2014). I has been ecen ly
e iew ha polyP may be a s ong ac i a o o he mi ochond ial pe meabili y ansi ion po e in
ca diomyce es, hea muscle cells, playing a s uc u al ole in hei mi ochond ia memb ane sys ems
(Dedko a and Bla e 2014; Seidlmaye e al. 2012a; Seidlmaye e al. 2012b).
2. PolyP as a Subs i u e o ATP
As phospho yla ed compound wi h a Gibbs ee ene gy o hyd olysis simila o ATP (-30.5 kJ mol−1), polyP
may ac as a subs i u e o ATP in di e se enzyma ic eac ions (Ko nbe g e al. 1999).
Dono o Suga s: PolyP-gluco(manno)kinase
Polyphospha e gluco(manno)kinase (PPGK; Polyphospha e-glucose phospho ans e ase, EC 2.7.1.63), a
membe o he ROK (Rep esso -ORF-Kinase) supe amily (P am PF00480), ca alyzes he phospho yla ion o
monosaccha ides –glucose, mannose, and in some cases uc ose– using polyP o ATP as a phospho yl dono .
PolyPn + D-glucose → PolyPn-1 + D-glucose-6-phospha e
This enzyma ic ac i i y has been epo ed in a a ie y o phylogene ically di e en bac e ia, including
impo an pa hogens (Szymona and Os owski 1964; Szymona and Szymona 1978), bac e ia o ac i a ed
sludge (Tanaka e al. 2003), and N2- ixing cyanobac e ia (Albi and Se ano 2015).
Dono o Adenyla e Kinases: NAD Kinase
NAD kinase ((polyP)/ATP:NAD 2’-phospho ans e ase, EC 2.7.1.23; P am PF01513) ca alyzes he
phospho yla ion o NAD o yield NADP. In some p oka yo es, NAD kinases use ei he ATP o polyP as
phospho yl dono s:
ATP + NAD → ADP + NADP
PolyPn + NAD → PolyPn-1 + NADP
PolyP ha e been pos ula ed as he p ecu so o ATP and he p imi i e ene gy dono in he o igin o li e
(Ko nbe g 1995; Lipmann 1965). Simila ly o ATP, polyP is composed by high-ene gy phospha e g oups and
i was likely p esen on p ebio ic ea h. Mo eo e , polyP o med by high p essu e and desicca ion (phospha e
condensa ion) migh ha e been na u ally abundan (sedimen a y ocks, hyd o he mal en s, olcanic
exuda es) in he ea ly ea h (Loh mann and O gel 1968; Mille and Pa is 1964). Based on hei compa able
chemical p ope ies and i s ubiqui y, we should no exclude a ole o polyP in ene gy p o ome abolism o
p imo dial cells (Achbe ge o a and Nahalka 2011; B own and Ko nbe g 2004). Fu he mo e, subsequen
biochemical s udies on bac e ial NAD kinases and glucokinases e ealed ha some o hem a e ac i e wi h
polyP. In pa icula , polyP can eally subs i u e o ATP, and some enzymes a e e en s ic ly dependen on
polyP. This hypo hesis is subs an ia ed by se e al la e obse a ions om he biochemical p ope ies o NAD
kinases and glucokinases: mos bac e ial enzymes a e able o use bo h phospho yl dono s wi h an obse ed
p og essi e dec ease in he p e e ence o polyP in he phylogene ically newe axa (Albi and Se ano 2015).
s ess esponses (Maciag e al. 2011). σ38 also con ols he algina e p oduc ion as well as swimming and
wi ching mo ili y in Pseudomonas ae uginosa. Simila ly, he σE egulon in Mycobac e ium spp. de e mines
he esponse o oxida i e and phospha e-limi ing s esses and is also equi ed o i ulence and pe sis ence o
his pa hogen (Manganelli e al. 2001).
9. S ess P o ec ion
Mic obial s a egies in esponse o oxida i e and o he s esses comp ise se e al mechanisms on pos -
ansla ional con ol, edox- egula ed adjus men o cellula me abolism, and he ac i a ion o speci ic
molecula chape ones. Recen ly, i was epo ed ha polyP exe s as a unc ional p o ein-p o ec i e chemical
chape one a physiological le els (G ay e al. 2014). Thus, polyP is able o s abilize a b oad ange o p o eins
main aining hei compe en con o ma ions, p e en ing hem om un olding and agg ega ion. In addi ion,
bac e ial ppk-null mu an s su e om highe p o ein damage han he wild- ype s ain upon a simila
p o eo oxic s ess. Besides, polyP may ha e some ad an ages compa ed o o he chape ones since i does no
eac wi h oxidan s, such as HClO, and does no equi e ATP hyd olysis o i s p o ec i e ac i i y (Kampinga
2014).
On he o he hand, polyP enhance Vib io chole ae cells ole ance o en i onmen al s esses in Pi-limi ing
condi ions (Jahid e al. 2006), and ppk-null mu an s o Lac obacillus spp. (Alcan a a e al. 2014) and E. coli
(G ay e al. 2014), which a e no able o p oduce polyP, show educed g ow h o a e mo e sensi i e o acidic
pH, e hanol, hea , high-sal and oxida i e s esses. Fu he mo e, i has been epo ed ha polyP p oduc ion by
bac e ia o he human gas oin es inal ac p o ec s he in es inal epi helia om oxida i e s ess (Segawa e al.
2011). To summa ize, hese esul s co obo a e he impo an con ibu ion o polyP o he egula ion o
g ow h, cell su i al and s ess ole ance o many mic oo ganisms.
PROSPECT

Despi e he iden i ica ion o polyP a he end o he nine een h cen u y and i s ex ensi e occu ence co e ing
he whole e olu iona y lineages, polyP was la gely dismissed and o go en du ing decades. Recen ly, he e is
an inc easing in e es in his polyme , which goes hand-in-hand wi h he e ela ion o i s unexpec ed and
in iguing in ol emen in c i ical cellula unc ions in p oka yo es and euka yo es. Thanks o hese s udies, i
has become e iden an ac i e associa ion be ween polyP and many physiological p ocesses o pa amoun
impo ance o mic oo ganisms, such as mul ilaye me abolic egula ion, s ess esponses, pa hogen
esis ance, e c. In a b oade con ex , polyP was also ecen ly epo ed o be in ol ed in a a ie y o biological
p ocesses ela ed o human heal h, such as ca diac ischaemia, blood coagula ion, apop osis and s ess-induced
cell dea h (Dedko a and Bla e 2014; He nandez-Ruiz e al. 2006; Seidlmaye e al. 2012b), sugges ing i s
he apeu ic use. The ecognized impo ance o such ecen ad ances, as well as he g owing numbe o
esea che s engaged in he s udy o polyP, shall os e o iginal and ascina ing p og esses and applica ions
ela ed o his ancien biopolyme in he nex u u e.
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FIGURE CAPTIONS
Figu e 1. Rep esen a i e schema ic s uc u es o he h ee main polyPs s uc u al classes. (a) Linea
polyphospha es, (b) cyclic polyphospha es (also named me aphospha es), and (c) b anched polyphospha es
(also named ul aphospha es).
Figu e 2. Func ions o polyPs in p oka yo ic and euka yo ic mic oo ganisms. In mos cases he indica ed
unc ions ha e been epo ed o bo h p oka yo es (bac e ia, a chaea) and euka yo es ( ungi, mic oalgae and
pa asi ic and ee-li ing he e o ophic p o is s).
Fig. 1
P O P O
O O
O P O
O
O O O
n
Linea polyphospha e
(a)
P O P
O
O P
O O O
O O
P O
O
O
P
B anched polyphospha e
(ul aphospha e)
(c)
Cyclic ipolyphospha e
(me aphospha e)
(b)
P O
O
O
P P
O O
O O
O O
Figu e 1 Click he e o download Figu e Figu e 1.pd