Abstract
Abstract Absorption, infrared, and 1H-NMR spectra of the ruthenium(II) octaethylporphine carbonyl complex [Ru(II)OEP·CO] were studied in the presence of alkanethiolate anion (−SR) as a model system for the reduced cytochrome P-450 carbonyl complex. The 1H-NMR spectra reveal that alkanethiolate anions coordinte toa the central metal atom of Ru(II)OEP·CO as the sixth ligand. The hexaccordinated complex [Ru(II)OEP·CO·−SR] has anomalous features as compared with the pentacoordinated complex [Ru(II)OEP·CO]: (1) the Soret band is splitted into two peaks, one in the near UV 363–365 nm region and the other in the 419–428 nm region, (2) the carbonyl stretching frequency is shifted by 25 cm−1 to lower wave number, (3) the proton signals of porphyrin ligand are shifted to higher magnetic field. Similarity of absorption and infrared spectra of the hexacoordinated complex to those of the reduced cytochrome P-450 carbonyl complex supports the axial ligation of the cysteinate to the central iron atom of the heme-proteins. The low wave number shifts of carbonyl stretching vibration and high field shifts of protons in the 1H-NMR spectra suggest the charge transfer interaction from 3p lone pair electrons of sulfur atom of alkanethiolate anion to the central metal and/or the porphyrin ligand.
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