Protein reduction-oxidation (redox) modification is an important mechanism that allows microorganisms to sense environmental changes and initiate cellular responses. We have developed a quantitative chemical probe approach for live cell labeling and imaging of proteins that are sensitive to redox modifications. We utilize this in vivo strategy to identify 176 proteins undergoing ~5-10 fold dynamic redox change in response to nutrient limitation and subsequent replenishment in the photoautotrophic cyanobacterium, Synechococcus sp. PCC 7002. We detect redox changes in as little as 30 seconds after nutrient perturbation, and oscillations in reduction and oxidation for 60 minutes following the perturbation. Many of the proteins undergoing dynamic redox transformations participate in the major components for the production (photosystems and electron transport chains) or consumption (Calvin-Benson cycle and protein synthesis) of reductant and/or energy in photosynthetic organisms. Thus, our in vivo approach reveals new redox-susceptible proteins and validates those previously identified in vitro.