SPECTRAL EVIDENCE FOR INTERACTIONS BETWEEN MEMBRANE-BOUND HEMES - RESONANCE RAMAN-SPECTRA OF MITOCHONDRIAL CYTOCHROME-B-C1 COMPLEX AS A FUNCTION OF REDOX POTENTIAL
SPECTRAL EVIDENCE FOR INTERACTIONS BETWEEN MEMBRANE-BOUND HEMES - RESONANCE RAMAN-SPECTRA OF MITOCHONDRIAL CYTOCHROME-B-C1 COMPLEX AS A FUNCTION OF REDOX POTENTIAL
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DOI:
10.1016/0014-5793(77)80438-9
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发表时间:
1977-01-01
期刊:
影响因子:
3.5
通讯作者:
ERECINSKA, M
中科院分区:
文献类型:
--
作者:
ADAR, F;ERECINSKA, M
Resonance Raman (RR) spectra of many hemeproteins [l-lo] and metalloporphyrins[1 l-161 have been reported since the initial analysis of the scattering enhanced by resonance between the laser frequency and porphyrin rr to n* transitions in cytochrome c by Spiro et al.[17]. Later, more detailed descriptions of the scattering phenomenon in both cytochrome c [18-201 and other metalloporphyrins [15, 16, 2 l] were presented and correlations were made between RR band frequencies and oxidation and spin states of the iron in various hemeproteins [6, 22, 23]. Moreover, the proposal was made that because of its high resolution capabilities, RR spectra could be exploited as a probe of interactions between hemes in functioning biological membranes [24]. A model study on the~-0x0 dimer of tetraphenylporphin indicated that this technique was indeed sensitive to heme aggregation.Our initial work on the succinate cytochrome c reductase showed it to be a fruitful system for RR study for a variety of reasons:(1) RR spectra of isolated cytochromes exhibit well-defined marker bands [7];(2) The RR quantum yields of ferrous cytochromes are unusually large (lo-‘)[25];(3) The spectroscopic characterization of the RR effect in ferrous cytochromes is highly developed [17-191.