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Resonance Raman Spectroscopy

  1. Roman S. Czernuszewicz,
  2. Marzena B. Zaczek

Published Online: 13 JUN 2008

DOI: 10.1002/0470862106.ia327

Encyclopedia of Inorganic Chemistry

Encyclopedia of Inorganic Chemistry

How to Cite

Czernuszewicz, R. S. and Zaczek, M. B. 2008. Resonance Raman Spectroscopy. Encyclopedia of Inorganic Chemistry. .

Author Information

  1. University of Houston, Houston, TX, USA

Publication History

  1. Published Online: 13 JUN 2008


Resonance Raman (RR) spectroscopy is an invaluable and widely used probe of structure and bonding for chromophoric transition metal centers in proteins and enzymes. The spectacular increase in detection sensitivity and selectivity of RR spectroscopy for vibrations that are localized in the absorbing center(s) of the molecule has revolutionized the vibrational spectroscopic field of bioinorganic systems. In this article, we explain the characteristics of RR spectra, emphasizing the kind of information that can be obtained and the rules for optimal resonance enhancement. We then discuss the applications of RR scattering to the study of structural dynamics of two different mononuclear metal-cysteinate sites, type-1 copper in cupredoxins and Fe(S-Cys)4 center in rubredoxins, using a combination of site-directed mutagenesis, production of isotopically labeled proteins, and cryogenic-temperature RR methods. These chromophores, involved in biological electron transport, have been very suitable subjects for RR studies because they exhibit strong absorption bands in the visible region due to (Cys)S [RIGHTWARDS ARROW] Cu(II) (∼625 nm) and (Cys)S [RIGHTWARDS ARROW] Fe(III) (∼500–570 nm) charge-transfer electronic transitions that facilitate the observation of resonantly enhanced Cu-and Fe-thiolate vibrations.


  • infrared;
  • Raman;
  • resonance Raman;
  • inelastic scattering of light;
  • Stokes radiation;
  • anti-Stokes radiation;
  • Franck-Condon scattering;
  • Herzberg-Teller scattering;
  • vibrational frequency;
  • Raman shift;
  • molecular polarizability;
  • selection rules;
  • metalloproteins;
  • blue copper proteins;
  • cupredoxin;
  • azurin;
  • iron-sulfur proteins;
  • rubredoxin;
  • rubrerythrin