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Resonance raman study of metal-formazans: A model for complexes of metalloenzymes with chelate inhibitors

✍ Scribed by Richard L. Petersen; James T. McFarland; Kenneth L. Watters


Publisher
Elsevier Science
Year
1978
Weight
725 KB
Volume
9
Category
Article
ISSN
0006-3061

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✦ Synopsis


The resonance Rarnan (RR) spectra of a series of triaryl formazans and several of their metal complexes have been recorded. The spectra of the free formazans display seveml bands of we& to medium intensity that are unaffected by physical state or metal complex formation.

However, strong bands in the 1050-1200 cm-l and 1330-1430 cm-' regions are sensitive to both the physical state of the formazan and to the formation of metal compleses. This observation, coupled with the intensity of these bands, leads to the conclusion that they are fundamentals of C-N, o-N, C=N, and N=N stretching character that are diagnostic of conformation of the formazpl linkage. The bands ascribed to v(C=N) and v(N=N) in the 1330-1430 cm-l region may also be used as indicators of the formation of metal complexes. rather than "closed" conformation on the enzyme surface. whereas the simple zinc complex is in the "closed" conformation.


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Surface-enhanced resonance Raman spectro
✍ M. Hidalgo; R. Montes; J.J. Laserna; A. RupΓ©rez πŸ“‚ Article πŸ“… 1996 πŸ› Elsevier Science 🌐 English βš– 711 KB

Surface-enhanced resonance Raman spectra @ERRS) of the complexes PAPH-Co(II), PAPH-Ni(II), PAPH-Fe(II), and PHEN-Fe(I1) (PAPH = 2-pyridine carboxyaldehyde 2-pyridylhydrazone and PHEN = l,lO-phenanthroline) adsorbed on silver colloid have been studied. Differences among SERS spectra of ligands and SE