TY  - JOUR
AU  - Poetsch, A.
AU  - Rexroth, S.
AU  - Heberle, J.
AU  - Link, T. A.
AU  - Dencher, N. A.
AU  - Seelert, H.
TI  - Characterisation of subunit II and its oligomer from spinach chloroplast ATP synthase
JO  - Biochimica et biophysica acta / Biomembranes
VL  - 1618
SN  - 0005-2736
CY  - Amsterdam
PB  - Elsevier
M1  - PreJuSER-32543
SP  - 59 - 66
PY  - 2003
N1  - Record converted from VDB: 12.11.2012
AB  - 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.
KW  - J (WoSType)
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000187163700008
DO  - DOI:10.1016/j.bbamem.2003.10.007
UR  - https://juser.fz-juelich.de/record/32543
ER  -