Resonance Raman study of reduced cytochromes.

<p>The RRS spectra of the studied cytochromes in the reduced state: WT—wild type; M1—T78N/K79Y/M80I/I81M/F82N, M2—T78S/K79P, M3—I81Y/A83Y/G84N. For clearer presentation, the spectra are shifted in vertical position. X axis is a frequency shift, cm^-1 and Y axis is RRS intensity, a.u.</p

The intensity ratios of selected peaks in the RRS spectra of the reduced wild-type cytochrome <i>c</i> and its mutants.

<p>Data are shown as mean values ± SE. *p<0.05 compared to wild-type cytochrome <i>c</i> (non-parametric Kruskal-Wallis test with Dunn's multiple comparison test).</p

The informational structure of horse cytochrome <i>c</i> and its mutant forms: Result of the analyzis of the amino acid sequence using the ANIS method.

<p>(A) The hierarchically organized highest rank ELIS (continuous lines) and the fragments of the bipartite graph that cannot be revealed using the ANIS method (dashed line). X axis is the size of the smoothing interval a/2 [<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0178280#pone.0178280.ref021" target="_blank">21</a>], Y axis is the number N of amino acid in the primary structure of horse cytochrome <i>c</i>; (B), (C), (D) The hierarchically organized highest rank ELIS in mutant forms T78S/K79P, I81Y/A83Y/G84N, T78N/K79Y/M80I/I81M/F82N, respectively; (E) The spatial structure of horse cytochrome <i>c</i> (1HRC.PDB). The highest rank ELIS in the spatial structure of cytochrome c are shown. His18 and Met 80 residues coordinated to the Fe atom are indicated. The ADD- site (P76-A83) with the abnormally low density of first rank ELIS is shown by the arrows.</p

SERS study of oxidized cytochromes.

<p><b>(A)</b> The SERS spectra of the studied cytochromes in the oxidized state: WT—wild type; M1—T78N/K79Y/M80I/I81M/F82N, M2—T78S/K79P, M3—I81Y/A83Y/G84N. For clearer presentation, the spectra are shifted in vertical position. Numbers above peaks indicate positions of their maxima used in the analysis. X axis is a frequency shift, cm^-1; Y axis is SERS intensity, a.u. (B) Structural formula of heme <i>c</i> with numeration of C atoms.</p

Comparison of the kinetic parameters of the succinate:cytochrome <i>c</i> reductase and cytochrome <i>c</i> oxidase reactions in rat liver mitoplasts in the presence of the externally added WT or mutant cytochromes <i>c</i>.

<p>The ratios of the maximum reaction rates in the presence of mutant forms of cytochrome <i>c</i> to the reaction rate in the presence of a WT protein <i>A</i>max(mut)/<i>A</i>max(wt) are also calculated.</p

The intensity ratios of selected peaks in the SERS spectra of oxidized wild-type cytochrome <i>c</i> and its mutants.

<p>Data are shown as mean values ± SE. *p<0.05 compared to wild-type cytochrome <i>c</i> (the non-parametric Kruskal-Wallis test with Dunn's multiple comparison test).</p

The structure of the oligonucleotides (direct primers) used to introduce mutations into a sequence of horse cytochrome <i>c</i>.

<p>The structure of the oligonucleotides (direct primers) used to introduce mutations into a sequence of horse cytochrome <i>c</i>.</p