1982
DOI: 10.1021/ja00380a006
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Structural correlations and vinyl influences in resonance Raman spectra of protoheme complexes and proteins

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Cited by 323 publications
(295 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: 72%
“…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: 72%
“…The optical spectra of the reduced proteins at high pH closely resemble those of ferrous cytochrome b 558 (44), a known bis-Hisligated protein (43,54). Moreover, the RR spectra of the oxidized and reduced MnP proteins are also similar to those of cytochrome b 558 and bis(imidazole) heme (42,43,59). Finally, the 5cHS species is restored upon addition of excess calcium at high pH.…”
Section: Discussionmentioning
confidence: 72%
“…A similar spectrum is observed in the F190I mutant MnP in 40 mM phosphate, pH 7.5 ( Figure 3), indicating that similar LS species are formed in the two proteins, although the transition occurs at lower pH in the mutant enzyme. Both spectra resemble RR spectra of ferric bis(imidazole) heme and ferric cytochrome b 558 (Table 2) (42,43). These data strongly suggest that the 6cLS species is formed by a rearrangement at the heme, which allows coordination of the distal imidazole, H46, resulting in a bis(histidyl) heme iron structure.…”
Section: Uv-vis and Rr Spectroscopy Of The Oxidized Proteinsmentioning
confidence: 83%
“…2(A)) are at 1502 cm À1 (m 3 ), 1584 cm À1 (m 2 ), and 1635 cm À1 (m 10 ). The pronounced saddling distortion of the heme group in the native structure [20] is manifested in the RR spectra by the lower frequencies of the core size marker bands compared to planar heme proteins, which display an inverse correlation between the RR band frequencies and the metalloporphyrin core size [22][23][24][25]. At pH 2.5 a net decrease of the intensity of the core size marker bands of the 6cLS heme is observed with the appearance of new bands at 1483, 1570 and 1620 cm À1 corresponding to a 6cHS species.…”
Section: Resonance Raman Spectroscopymentioning
confidence: 99%