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Chlorina and viridis mutants of barley ( Hordeum vulgare L.) allow assignment of long‐wavelength chlorophyll forms to individual Lhca proteins of photosystem I in vivo
Author(s) -
Knoetzel Jürgen,
Bossmann Björn,
Grimme L.Horst
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)01158-2
Subject(s) - hordeum vulgare , photosystem ii , fluorescence , photosystem i , chlorophyll , mutant , chemistry , p700 , photosynthesis , chlorophyll a , chlorophyll fluorescence , photosynthetic reaction centre , photochemistry , biology , botany , biochemistry , poaceae , physics , optics , gene
The isolated subcomplex LHCI‐730 of plant photosystem I (PSI) chlorophyll (Chl) a / b binding antenna is a heterodimer of Lhca1 and Lhca4 and has a 77 K fluorescence emission peak at 730 nm (F730). Recently, three Chl spectral forms with 77 K fluorescence emission peaks at 720 nm, 730 nm and 742 nm were identified in native PSI. In an attempt to assign the two longest wavelength emission maxima to peripheral PSI antenna proteins, we performed 77 K fluorescence emission spectroscopy on intact leaves of chlorina and viridis mutants from barley which lack individual LHCI‐730 proteins. This approach indicates that F732 is found only in Lhca1 and F742 only in Lhca4, when these proteins are associated with the PSI reaction centre.