Effects of Protein Structure on Iron–Polypeptide Vibrational Dynamic Coupling in Cytochrome c

Galinato, Mary Grace I.; Bowman, Sarah E.  J.; Kleingardner, Jesse G.; Martin, Sherri; Zhao, Jiyong; Sturhahn, Wolfgang; Alp, E. Ercan; Bren, Kara L.; Lehnert, Nicolai

doi:10.1021/bi501430z

Title: Effects of Protein Structure on Iron–Polypeptide Vibrational Dynamic Coupling in Cytochrome c

Journal Article · Mon Dec 22 00:00:00 EST 2014 · Biochemistry

DOI:https://doi.org/10.1021/bi501430z· OSTI ID:1261133

Galinato, Mary Grace I. ^[1]; Bowman, Sarah E. J. ^[2]; Kleingardner, Jesse G. ^[2]; Martin, Sherri ^[3]; Zhao, Jiyong ^[4]; Sturhahn, Wolfgang ^[4]; Alp, E. Ercan ^[4]; Bren, Kara L. ^[2]; Lehnert, Nicolai ^[3]

Univ. of Michigan, Ann Arbor, MI (United States). Dept. of Chemistry; Penn State, Erie, PA (United States). Behrend College
Univ. of Rochester, NY (United States). Dept. of Chemistry
Univ. of Michigan, Ann Arbor, MI (United States). Dept. of Chemistry
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)

Cytochrome c (Cyt c) has a heme covalently bound to the polypeptide via a Cys-X-X-Cys-His (CXXCH) linker that is located in the interface region for protein-protein interactions. To determine whether the polypeptide matrix influences iron vibrational dynamics, nuclear resonance vibrational spectroscopy (NRVS) measurements were performed on Fe-57-labeled ferric Hydrogenobacter thermophilus cytochrome c-552, and variants M13V, M13V/K22M, and A7F, which have structural modifications that alter the composition or environment of the CXXCH pentapeptide loop. Simulations of the NRVS data indicate that the 150-325 cm(-1) region is dominated by N-His-Fe-S-Met axial ligand and polypeptide motions, while the 325-400 cm(-1) region shows dominant contributions from nu(Fe-N-Pyr) (Pyr = pyrrole) and other heme-based modes. Diagnostic spectral signatures that directly relate to structural features of the heme active site are identified using a quantum chemistry-centered normal coordinate analysis (QCC-NCA). In particular, spectral features that directly correlate with CXXCH loop stiffness, the strength of the Fe-His interaction, and the degree of heme distortion are identified. Cumulative results from our investigation suggest that compared to the wild type (wt), variants M13V and M13V/K22M have a more rigid CXXCH pentapeptide segment, a stronger Fe-N-His interaction, and a more ruffled heme. Conversely, the A7F variant has a more planar heme and a weaker Fe-N-His bond. These results are correlated to the observed changes in reduction potential between wt protein and the variants studied here. Implications of these results for Cyt c biogenesis and electron transfer are also discussed.

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Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States)

Sponsoring Organization:: National Institutes of Health (NIH); USDOE Office of Science (SC), Basic Energy Sciences (BES)

Grant/Contract Number:: R01-GM63170; AC02-06CH11357

OSTI ID:: 1261133

Alternate ID(s):: OSTI ID: 1362102

Journal Information:: Biochemistry, Vol. 54, Issue 4; ISSN 0006-2960

Publisher:: American Chemical Society (ACS)Copyright Statement

Country of Publication:: United States

Language:: English

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Cited by: 8 works

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