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Mpe reductase (4VMpeR) in greening barley etiochloroplasts (Kolossov and
Rebeiz
2010
). Such etiochloroplasts can actively convert MV Mpe to MV Pchlide
a
(Tripathy and Rebeiz
1986
).
Biosynthesis of MV Pchlide a in DMV-LDV-LDMV Plant Species via Routes 12
MV Pchlide
a
is formed via biosynthetic route 12 fromMV Mg-Proto and MV Mpe
(Fig.
8.8
). Indeed in green DMV-LDV-LDMV plants MV Pchlide
a
formation is
very active (Abd-El-Mageed et al.
1997
) and barley etiochloroplasts are capable of
strongly converting MV Mpe to MV Pchlide
a
(Tripathy and Rebeiz
1986
).
8.2 Pchlide-Protein Complexes
Further metabolism of DV and MV Pchlide
a
takes place only if the Pchlide is
complexed to an apoprotein. The Pchlide-apoprotein complex is referred to as a
Pchl-holochrome (Pchl-Hs). Various Pch-Hs holochromes will be discussed in
detail below.
8.2.1 Heterogeneity of Pchlide a-Protein Complexes
As we have mentioned previously, Pchlides
a
are chemically heterogeneous. That
heterogeneity is expressed chemically as DV, and MV substitutions at the level of
the tetrapyrrole chromophore at position 4 of the macrocycle. It is also expressed at
the level of the esterifying group at position 7 of the macrocycle as will be discussed
most cases the chromophore of Pchl-Hs consist mostly of Pchlide
a
and much
holochromes as Pchl(ide)-Hs. The overall heterogeneity is also expressed by the
detection of multiple resonance excitation energy transfer bands between Pchl(ide)-
Discussion of the heterogeneity of Pchl(ide)-Hs will focus (a) on the possible
nature of the chromophore-apoprotein association, (b) on the spectroscopic
properties of various Pchl(ide)
a
-Hs
in situ
, and (c) on the properties of purified
Pchl(ide)-Hs.
8.2.1.1 Nature of the Chromophore-Protein Association of Pchl(ide)-Hs
In etiolated tissues, Pchlide
a
is the most abundant tetrapyrrole (90-95 %) followed
by less abundant Pchlide
a
ester (Pchlide
a
E) (5-10 %) (Rebeiz et al.
1970
).
Pchlide
a
and its ester will be referred to collectively as Pchl(ide)
a
. Upon binding
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