Related Experiment Video
Updated: Oct 7, 2026

A New Approach for the Comparative Analysis of Multiprotein Complexes Based on 15N Metabolic Labeling and Quantitative Mass Spectrometry
Published on: March 13, 2014
Interaction of sulfite with the noncatalytic and catalytic sites of chloroplast coupling factor cf1
1Institute of Basic Biological Problems, Russian Academy of Sciences, Pushchino, Moscow Region, 142290, Russia. Malyan@issp.serpukhov.su
Abstract:
The interaction between sulfite, an efficient Mg2+-dependent F1-ATPase activator, and chloroplast CF1-ATPase was studied. The sulfite anion was shown to inhibit ADP and ATP binding to the noncatalytic sites of CF1. The stimulating activity of sulfite persists when all noncatalytic sites are nucleotide-occupied. Phosphate, a competing candidate for binding to CF1 catalytic sites, suppresses this activity. These results support the suggestion that the stimulation of Mg2+-dependent ATPase activity of CF1 is caused by sulfite binding to its catalytic sites.
Related Concept Videos
Sulfur Assimilation
Electron Transport Chain: Complex III and IV
The Supercomplexes in the Crista Membrane
Electron Transport Chain: Complex I and II
ROS generation is regulated and maintained at moderate levels necessary...
The Z-Scheme of Electron Transport in Photosynthesis
The Photochemical Reaction Center