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Title: Crystallization of the c[subscript 14]-rotor of the chloroplast ATP synthase reveals that it contains pigments

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 phosphage, 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 (c{sub 10-14}{gamma}{sup {epsilon}}) relative to stator moiety ({alpha}{sub 3}{beta}{sub 3}{delta}ab{sub 2}). Here we report the isolation and crystallization of the c{sub 14}-ring of subunit c from the spinach chloroplast enzyme diffracting as far as 2.8 {angstrom}. Though ATP synthase was not previously know to contain any pigments, the crystals of the c-subunit possessed a strong yellow color. The pigment analysis revaled 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.

Authors:
; ; ;  [1]
  1. AZU
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
USDOE
OSTI Identifier:
1006692
Resource Type:
Journal Article
Journal Name:
BBA-Bioenergetics
Additional Journal Information:
Journal Volume: 1777; Journal Issue: (7-8) ; 07, 2008; Journal ID: ISSN 0005-2728
Country of Publication:
United States
Language:
ENGLISH
Subject:
59 BASIC BIOLOGICAL SCIENCES; 60 APPLIED LIFE SCIENCES; ADP; ATP; CAROTENOIDS; CHLOROPHYLL; CHLOROPLASTS; COLOR; CRYSTALLIZATION; CRYSTALS; ENZYMES; FUNCTIONS; PIGMENTS; POTENTIALS; PROTEINS; PROTONS; RINGS; ROTATION; ROTORS; SPINACH; STATORS; SYNTHESIS

Citation Formats

Varco-Merth, Benjamin, Fromme, Raimund, Wang, Meitian, and Fromme, Petra. Crystallization of the c[subscript 14]-rotor of the chloroplast ATP synthase reveals that it contains pigments. United States: N. p., 2008. Web. doi:10.1016/j.bbabio.2008.05.009.
Varco-Merth, Benjamin, Fromme, Raimund, Wang, Meitian, & Fromme, Petra. Crystallization of the c[subscript 14]-rotor of the chloroplast ATP synthase reveals that it contains pigments. United States. https://doi.org/10.1016/j.bbabio.2008.05.009
Varco-Merth, Benjamin, Fromme, Raimund, Wang, Meitian, and Fromme, Petra. 2008. "Crystallization of the c[subscript 14]-rotor of the chloroplast ATP synthase reveals that it contains pigments". United States. https://doi.org/10.1016/j.bbabio.2008.05.009.
@article{osti_1006692,
title = {Crystallization of the c[subscript 14]-rotor of the chloroplast ATP synthase reveals that it contains pigments},
author = {Varco-Merth, Benjamin and Fromme, Raimund and Wang, Meitian and Fromme, Petra},
abstractNote = {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 phosphage, 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 (c{sub 10-14}{gamma}{sup {epsilon}}) relative to stator moiety ({alpha}{sub 3}{beta}{sub 3}{delta}ab{sub 2}). Here we report the isolation and crystallization of the c{sub 14}-ring of subunit c from the spinach chloroplast enzyme diffracting as far as 2.8 {angstrom}. Though ATP synthase was not previously know to contain any pigments, the crystals of the c-subunit possessed a strong yellow color. The pigment analysis revaled 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.},
doi = {10.1016/j.bbabio.2008.05.009},
url = {https://www.osti.gov/biblio/1006692}, journal = {BBA-Bioenergetics},
issn = {0005-2728},
number = (7-8) ; 07, 2008,
volume = 1777,
place = {United States},
year = {Wed Aug 27 00:00:00 EDT 2008},
month = {Wed Aug 27 00:00:00 EDT 2008}
}