Resonance Raman Characterization of O2-Binding Heme Proteins.

Samuel N Snyder, Tapiwa Chiura, Piotr J Mak

Methods in molecular biology (Clifton, N.J.) 2023

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A vast array of critical in vivo processes and pathways are dependent on a multitude of O2-binding heme proteins which contain a diverse range of functions. Resonance Raman (rR) spectroscopy is an ideal technique for structural investigation of these proteins, providing information about the geometry of the Fe-O-O fragment and its electrostatic interactions with the distal active site. Characterization of these oxy adducts is an endeavor that is complicated by their instability for many heme proteins in solution, an obstacle which can be overcome by applying the rR technique to cryogenically frozen samples. We describe here how to measure rR spectra of heme proteins with stable oxy forms, as well as the technical adaptations required to measure unstable samples at 77 K. © 2023. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.

Citation

Samuel N Snyder, Tapiwa Chiura, Piotr J Mak. Resonance Raman Characterization of O2-Binding Heme Proteins. Methods in molecular biology (Clifton, N.J.). 2023;2648:27-41