%0 Journal Article
%A Poetsch, A.
%A Rexroth, S.
%A Heberle, J.
%A Link, T. A.
%A Dencher, N. A.
%A Seelert, H.
%T Characterisation of subunit II and its oligomer from spinach chloroplast ATP synthase
%J Biochimica et biophysica acta / Biomembranes
%V 1618
%@ 0005-2736
%C Amsterdam
%I Elsevier
%M PreJuSER-32543
%P 59 - 66
%D 2003
%Z Record converted from VDB: 12.11.2012
%X Proton ATP synthases carry out energy conversion in mitochondria, chloroplasts, and bacteria. A key element of the membrane integral motor CFO in chloroplasts is the oligomer of subunit III: it converts the energy of a transmembrane electrochemical proton gradient into rotational movement. To enlighten prominent features of the structure-function relationship of subunit III from spinach chloroplasts, new isolation methods were established to obtain highly pure monomeric and oligomeric subunit III in milligram quantities. By Fourier-transform infrared (FTIR) and CD spectroscopy, the predominantly a-helical secondary structure of subunit III was demonstrated. For monomeric subunit III, a conformational change was observed when diluting the SDS-solubilized protein. Under the same conditions the conformation of the oligomer III did not change. A mass of 8003 Da for the monomeric subunit III was determined by MALDI mass spectrometry (MALDI-MS), showing that no posttranslational modifications occurred. By ionisation during MALDI-MS, the noncovalent homooligomer III14 disaggregated into its III monomers. (C) 2003 Elsevier B.V All rights reserved.
%K J (WoSType)
%F PUB:(DE-HGF)16
%9 Journal Article
%U <Go to ISI:>//WOS:000187163700008
%R 10.1016/j.bbamem.2003.10.007
%U https://juser.fz-juelich.de/record/32543