Abstract:
:Purified cytochrome c oxidase CO complex from beef heart has been studied by Fourier transform infrared absorbance difference spectroscopy. Photolysis at 10-20 Kelvin results in dissociation of a3FeCO, formation of CuBCO, and perturbation of the a3-heme and CuB complex. The vibrational perturbation spectrum between 900 and 1700 cm-1 contains a wealth of information about the binuclear center. Appearance in infrared photoperturbation difference spectra of virtually all bands previously reported from resonance Raman spectra indicate the importance of polarization along the 4-vinyl:8-formyl axis, which results in the reduction of heme symmetry to C2v. Frequency-shifted bands due to the 8-formyl and 4-vinyl groups of the a3-heme have been identified and quantitated. The frequency shifts have been interpreted as being due to a change in porphyrin polarization with change in spin state of the iron by photodissociation of CO or perturbation of the CuB coordination complex.
journal_name
Biophys Jjournal_title
Biophysical journalauthors
Park S,Pan LP,Chan SI,Alben JOdoi
10.1016/S0006-3495(96)79304-9subject
Has Abstractpub_date
1996-08-01 00:00:00pages
1036-47issue
2eissn
0006-3495issn
1542-0086pii
S0006-3495(96)79304-9journal_volume
71pub_type
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