1975
DOI: 10.1021/ja00842a032
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Resonance Raman spectra of metallooctaethylporphyrins. Structural probe of metal displacement

Abstract: Comparison of resonance Raman spectra of Ddh and Did molecular forms of octaethylporphinatonickel(Il) (NiOEP) indicates high-frequency bands at 1660, 1609, 1581, and 1524 cm-1 are structure-sensitive. Upon deuteration at the meso carbons two additional anomalously polarized bands appear with a concomitant decrease in intensity of the 1310-cm_1 anomalously polarized line. The spectrum in solution is consistent with a planar NiOEP structure. Spectra of CuOEP imply the existence of two molecular forms in this com… Show more

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Cited by 238 publications
(168 citation statements)
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“…Similar changes have been previously observed also upon binding of ferric horse cyt-c to anionic dioleoyl-phosphatidylglycerol (DOPG) vesicles [29]. The pronounced saddle-distortion [30] of the heme group in native cyt c is responsible of the lower core size marker bands frequencies in the RR spectrum compared to planar heme proteins, which display an inverse correlation between RR band frequencies and the porphyrin core size [31][32][33]. Therefore, the upshift in the RR bands observed upon CL binding is indicative of the conversion to a more planar heme.…”
Section: The (Cyt C-cl Liposome) Interactionsupporting
confidence: 74%
“…Similar changes have been previously observed also upon binding of ferric horse cyt-c to anionic dioleoyl-phosphatidylglycerol (DOPG) vesicles [29]. The pronounced saddle-distortion [30] of the heme group in native cyt c is responsible of the lower core size marker bands frequencies in the RR spectrum compared to planar heme proteins, which display an inverse correlation between RR band frequencies and the porphyrin core size [31][32][33]. Therefore, the upshift in the RR bands observed upon CL binding is indicative of the conversion to a more planar heme.…”
Section: The (Cyt C-cl Liposome) Interactionsupporting
confidence: 74%
“…Excitation within the Soret region enhances symmetric modes of vibration within the porphyrin (55). The modes ν 3 , ν 10 , and ν 2 are primary RR marker bands that characterize spin state, a measure of the pyrrole nitrogen-carbon stretching frequencies within the porphyrin core that respond to changes in the iron spin (56). The RR spectra of the ferric wild-type and F190I mutant MnP are very similar (Figure 3, Table 1), indicating that the FIGURE 6: High-frequency region of the resonance Raman spectra of reduced MnP under conditions used in Figure 3.…”
Section: Discussionmentioning
confidence: 99%
“…6c) display a progressive upshift of the bands upon addition of CL in the CL to cytochrome c ratio interval between 3 and 5, after which no further variations are observed. The pronounced saddling distortion of the wild-type protein [33] is reflected in the resonance Raman spectrum by lower core size marker band frequencies compared with planar heme proteins, which display an inverse correlation between resonance Raman band frequencies and the porphyrin core size [34][35][36]. Hence, interaction of CL with cytochrome c gives rise to a less distorted heme.…”
Section: The Asn52ile Mutant-cl Liposome Interactionmentioning
confidence: 99%