Evidence from biosynthetically incorporated strontium and FTIR difference spectroscopy that the C-terminus of the D1 polypeptide of photosystem II does not ligate calcium

Melodie A. Strickler, Lee M. Walker, Warwick Hillier, Richard J. Debus*

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    97 Citations (Scopus)

    Abstract

    Recent FTIR studies have provided evidence that the C-terminal α-COO- group of the D1 polypeptide at D1-Ala344 is a unidentate ligand of a Mn ion in photosystem II [Chu, H.-A., Hiller, W., and Debus, R. J. (2004) Biochemistry 43, 3152-3166; Kimura, Y., Mizusawa, N., Yamanari, T., Ishii, A., and Ono, T.-A. (2005) J. Biol. Chem. 280, 2078-2083], However, the FTIR data could not exclude Ca ligation. Furthermore, the recent ∼3.5 Å X-ray crystallographic structural model positions the α-COO - group of D1-Ala344 near a Ca ion [Ferreira, K. N., Iverson, T. M., Maghlaoui, K., Barber, J., and Iwata, S. (2004) Science 303, 1831-1838]. Therefore, to conclusively establish whether the α-COO- group of D1-Ala344 ligates Mn or Ca, the symmetric carboxylate stretching mode of the α-COO-1 group of D1-Ala344 was identified in the S 2-minus-S1 FTIR difference spectrum of PSII particles having Sr substituted for Ca. Cells of the cyanobacterium Synechocystis sp. PCC 6803 were propagated in media having Sr substituted for Ca and containing either L-[1-13C]alanine or unlabeled (12C) alanine. The S 2-minus-S1 FTIR difference spectra of the purified PSII particles show that substituting Sr for Ca alters several carboxylate stretching modes, including some that may correspond to one or more metal ligands, but importantly does not alter the symmetric carboxylate stretching mode of the α-COO-group of D1-Ala344. In unlabeled PSII particles, this mode appears at ∼1356 cm-1 in the S1 state and at either ∼1337 or ∼1320 cm-1 in the S2 state, irrespective of whether the PSII particles contain Ca or Sr. These data are inconsistent with Ca ligation and show, therefore, that the C-terminal α-COO- group of the D1 polypeptide ligates a Mn ion. These data also show that substituting Ca with the larger Sr ion perturbs other unidentified carboxylate groups, at least one of which may ligate the Mn 4 cluster.

    Original languageEnglish
    Pages (from-to)8571-8577
    Number of pages7
    JournalBiochemistry
    Volume44
    Issue number24
    DOIs
    Publication statusPublished - 21 Jun 2005

    Fingerprint

    Dive into the research topics of 'Evidence from biosynthetically incorporated strontium and FTIR difference spectroscopy that the C-terminus of the D1 polypeptide of photosystem II does not ligate calcium'. Together they form a unique fingerprint.

    Cite this