Probing Cytochrome c Folding Transitions upon Phototriggered Environmental Perturbations Using Time-Resolved X-ray Scattering

Rimmerman, Dolev; Leshchev, Denis; Hsu, Darren J.; Hong, Jiyun; Abraham, Baxter; Henning, Robert; Kosheleva, Irina; Chen, Lin X.

doi:10.1021/acs.jpcb.8b03354

Probing Cytochrome c Folding Transitions upon Phototriggered Environmental Perturbations Using Time-Resolved X-ray Scattering

Journal Article · 30 April 2018 · Journal of Physical Chemistry. B, Condensed Matter, Materials, Surfaces, Interfaces and Biophysical Chemistry

DOI:https://doi.org/10.1021/acs.jpcb.8b03354· OSTI ID:1473619

Rimmerman, Dolev ^[1]; Leshchev, Denis ^[1]; Hsu, Darren J. ^[1]; Hong, Jiyun ^[1]; Abraham, Baxter ^[2]; Henning, Robert ^[3]; Kosheleva, Irina ^[3]; ^[4]

Department of Chemistry, Northwestern University, Evanston, Illinois 60208, United States
Department of Chemistry and Biochemistry, University of Delaware, Newark, Delaware 19716, United States
Center for Advanced Radiation Sources, The University of Chicago, Chicago, Illinois 60637, United States
Department of Chemistry, Northwestern University, Evanston, Illinois 60208, United States; Chemical Sciences and Engineering Division, Argonne National Laboratory, Argonne, Illinois 60439, United States

Direct tracking of protein structural dynamics during folding–unfolding processes is important for understanding the roles of hierarchic structural factors in the formation of functional proteins. As such, using cytochrome c (cyt c) as a platform, we investigated its structural dynamics during folding processes triggered by local environmental changes (i.e., pH or heme iron center oxidation/spin/ligation states) with time-resolved X-ray solution scattering measurements. Starting from partially unfolded cyt c, a sudden pH drop initiated by light excitation of a photoacid caused a structural contraction in microseconds, followed by active site restructuring and unfolding in milliseconds. In contrast, the reduction of iron in the heme via photoinduced electron transfer did not affect conformational stability at short timescales (<1 ms), despite active site coordination geometry changes. These results demonstrate how different environmental perturbations can change the nature of interaction between the active site and protein conformation, even within the same metalloprotein, which will subsequently affect the folding structural dynamics.

Research Organization:: Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES)

DOE Contract Number:: AC02-06CH11357

OSTI ID:: 1473619

Journal Information:: Journal of Physical Chemistry. B, Condensed Matter, Materials, Surfaces, Interfaces and Biophysical Chemistry, Vol. 122, Issue 20; ISSN 1520-6106

Publisher:: American Chemical Society

Country of Publication:: United States

Language:: English

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