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. Author manuscript; available in PMC: 2022 Nov 18.
Published in final edited form as: J Phys Chem B. 2021 Nov 8;125(45):12401–12412. doi: 10.1021/acs.jpcb.1c05820

Figure 3.

Figure 3.

Experimentally tracking photolyzed ligation of heme protein. (a) Scheme of the cytochrome c heme active site. XTA tracks the local heme structural dynamics, and TRXSS tracks the global conformational changes. (b) Difference signal kinetics from XTA (edge and post-edge) overlaid with those from TRXSS (SAXS and WAXS). The post-edge and WAXS signatures correspond to the same process, bridging the spatial and temporal extents of the experiment. (c) Species-associated difference (SAD) on the left and their corresponding relative measured population on the right for the two intermediates, UM and UH, and the final unfolded state, FM. Reproduced from ref 60 with permission from the Royal Society of Chemistry.