Abstract
The ATP synthase is one of the most important enzymes on earth as it couples the transmembrane electrochemical potential of protons to the synthesis of ATP from ADP and inorganic phosphate, providing the main ATP source of almost all higher life on earth. During ATP synthesis, stepwise protonation of a conserved carboxylate on each protein subunit of an oligomeric ring of 10-15 c-subunits is commonly thought to drive rotation of the rotor moiety (c10-14γe{open}) relative to stator moiety (α3β3δab2). Here we report the isolation and crystallization of the c14-ring of subunit c from the spinach chloroplast enzyme diffracting as far as 2.8 Å. Though ATP synthase was not previously known to contain any pigments, the crystals of the c-subunit possessed a strong yellow color. The pigment analysis revealed that they contain 1 chlorophyll and 2 carotenoids, thereby showing for the first time that the chloroplast ATP synthase contains cofactors, leading to the question of the possible roles of the functions of the pigments in the chloroplast ATP synthase.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 605-612 |
| Number of pages | 8 |
| Journal | Biochimica et Biophysica Acta - Bioenergetics |
| Volume | 1777 |
| Issue number | 7-8 |
| DOIs | |
| State | Published - Jul 2008 |
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Keywords
- ATP synthase
- Carotenoid
- Chlorophyll
- Crystallization
- Membrane proteins
ASJC Scopus subject areas
- Biophysics
- Medicine(all)
Cite this
Crystallization of the c14-rotor of the chloroplast ATP synthase reveals that it contains pigments. / Varco-Merth, Benjamin; Fromme, Raimund; Wang, Meitian; Fromme, Petra.
In: Biochimica et Biophysica Acta - Bioenergetics, Vol. 1777, No. 7-8, 07.2008, p. 605-612.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Crystallization of the c14-rotor of the chloroplast ATP synthase reveals that it contains pigments
AU - Varco-Merth, Benjamin
AU - Fromme, Raimund
AU - Wang, Meitian
AU - Fromme, Petra
PY - 2008/7
Y1 - 2008/7
N2 - The ATP synthase is one of the most important enzymes on earth as it couples the transmembrane electrochemical potential of protons to the synthesis of ATP from ADP and inorganic phosphate, providing the main ATP source of almost all higher life on earth. During ATP synthesis, stepwise protonation of a conserved carboxylate on each protein subunit of an oligomeric ring of 10-15 c-subunits is commonly thought to drive rotation of the rotor moiety (c10-14γe{open}) relative to stator moiety (α3β3δab2). Here we report the isolation and crystallization of the c14-ring of subunit c from the spinach chloroplast enzyme diffracting as far as 2.8 Å. Though ATP synthase was not previously known to contain any pigments, the crystals of the c-subunit possessed a strong yellow color. The pigment analysis revealed that they contain 1 chlorophyll and 2 carotenoids, thereby showing for the first time that the chloroplast ATP synthase contains cofactors, leading to the question of the possible roles of the functions of the pigments in the chloroplast ATP synthase.
AB - The ATP synthase is one of the most important enzymes on earth as it couples the transmembrane electrochemical potential of protons to the synthesis of ATP from ADP and inorganic phosphate, providing the main ATP source of almost all higher life on earth. During ATP synthesis, stepwise protonation of a conserved carboxylate on each protein subunit of an oligomeric ring of 10-15 c-subunits is commonly thought to drive rotation of the rotor moiety (c10-14γe{open}) relative to stator moiety (α3β3δab2). Here we report the isolation and crystallization of the c14-ring of subunit c from the spinach chloroplast enzyme diffracting as far as 2.8 Å. Though ATP synthase was not previously known to contain any pigments, the crystals of the c-subunit possessed a strong yellow color. The pigment analysis revealed that they contain 1 chlorophyll and 2 carotenoids, thereby showing for the first time that the chloroplast ATP synthase contains cofactors, leading to the question of the possible roles of the functions of the pigments in the chloroplast ATP synthase.
KW - ATP synthase
KW - Carotenoid
KW - Chlorophyll
KW - Crystallization
KW - Membrane proteins
UR - http://www.scopus.com/inward/record.url?scp=49149117541&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=49149117541&partnerID=8YFLogxK
U2 - 10.1016/j.bbabio.2008.05.009
DO - 10.1016/j.bbabio.2008.05.009
M3 - Article
C2 - 18515064
AN - SCOPUS:49149117541
VL - 1777
SP - 605
EP - 612
JO - Biochimica et Biophysica Acta - Bioenergetics
JF - Biochimica et Biophysica Acta - Bioenergetics
SN - 0005-2728
IS - 7-8
ER -