We present a study of low concentration Fe͑III͒ doping in crystalline L-alanine by means of electron paramagnetic resonance, resonant Raman scattering, and photoluminescence. The magnetic resonance experiments show that Fe͑III͒ occupies two inequivalent sites of rhombic symmetry in the L-alanine crystal. We obtain for the principal directions of the effective giromagnetic tensor the values g z ϭ1.881(5), g y ϭ4.641(8), and g x ϭ7.238(5). In the optical experiments we find a selective resonant enhancement of some of the Raman active lattice vibrations comprising displacements of the hydrogen bonds between the carboxyl and ammonium groups of neighboring molecules. Based on these results we discuss the possible localization of the impurity in the crystal. ͓S0163-1829͑99͒06401-2͔
I. MOTIVATIONOrganometallic compounds play an important role in the biological functions of organisms. In contrast to carbon, hydrogen, oxygen, and nitrogen, metals exist in rather tiny proportions in biomolecules. Their existence is, notwithstanding, essential for some of the most important functions that proteins undertake in living matter. 1 The reversible binding of molecular oxygen carried off by the prosthetic heme group in myoglobin and hemoglobin is one important example. In this latter example, iron ͑Fe͒ can be observed either as divalent ͑oxyhemoglobin͒ or trivalent ͑ferrihemoglo-bin͒ depending on the experimental conditions. Metals serve also as cofactors of many enzymes; most enzyme classes include metal-dependent enzymes. Metalproteins are complex examples of interactions between metals and aminoacids. Simpler prototypes can be obtained by metal containing polyaminoacids or metal-aminoacid crystals. Their physics is not directly applicable to the properties of proteins and enzymes but rather constitute important model examples where a better understanding of the interaction between metals and aminoacids can be foretold. The study of their magnetic and electronic properties strives to obtain valuable information on the behavior of these ions in biologically relevant macromolecules. Copper ͑Cu͒ has played an important role in the study of metal-aminoacid single crystals. 2 Cu-doped L-alanine crystals have been extensively studied by electron paramagnetic resonance ͑EPR͒ and electron-nuclear double resonance ͑ENDOR͒ spectroscopy, leading to a detailed description of the site occupied by the impurities and their interactions with the ligands. 3 On the other hand, though Fe is one of the most important transition metal ions in living organisms, Fe-doped aminoacid crystals have not been studied to the same extent. In fact, the crystal structure revealing the position of the Fe impurities and their interactions with the molecular field of the crystal have not been, to the best of our knowledge, heretofore clearly worked out. The reasons for this lack of experimental information may be threefold. First, Fe impurities are accepted in rather low concentrations in aminoacid single crystals and, in any case, the crystal growth process is fa...