Abstract
The excited state properties of porphyrins have attracted considerable attention due to their relevance to the understanding of electron transfer processes in biological systems. The excited state porphyrins can transfer electrons in model systems such as the porphyrin derivatives of Ni(II), Cu(II), Mg(II), Ag(II), Zn(II), Pd(I1) and Pt(I1) [l-5]. In the report [6] on the steady-state and time-resolved luminescence emission in copper cytochrome c, intramolecular rate parameters below 80 K were significantly influenced by the porphyrin-protein interaction. Another application of substituted porphyrins is the study of the whole molecule rotational motion in membrane systems. [6]. The triplet state of rhodium-substituted cytochrome b5 was examined and its properties used to measure the rotational diffusion of the molecule in phospholipid vesicle system [ 71. Here we report the results of our measurements of decay time of transient triplet absorption and phosphorescence emission in zinc cytochrome c. It is known that zinc porphyrins can transfer electrons in the excited state in model systems [8]. We aim to investigate whether similar electron transfer occurs in proteins containing zinc-substituted porphyrins.
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