This title appears in the Scientific Report :
2003
Please use the identifier:
http://dx.doi.org/10.1016/j.bbamem.2003.10.007 in citations.
Characterisation of subunit II and its oligomer from spinach chloroplast ATP synthase
Characterisation of subunit II and its oligomer from spinach chloroplast ATP synthase
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 enligh...
Saved in:
Personal Name(s): | Poetsch, A. |
---|---|
Rexroth, S. / Heberle, J. / Link, T. A. / Dencher, N. A. / Seelert, H. | |
Contributing Institute: |
Biologische Strukturforschung; IBI-2 |
Published in: | Biochimica et biophysica acta / Biomembranes, 1618 (2003) S. 59 - 66 |
Imprint: |
Amsterdam
Elsevier
2003
|
Physical Description: |
59 - 66 |
DOI: |
10.1016/j.bbamem.2003.10.007 |
Document Type: |
Journal Article |
Research Program: |
Neurowissenschaften |
Series Title: |
BBA - Biomembranes
1618 |
Subject (ZB): | |
Publikationsportal JuSER |
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520 | |a 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. | ||
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