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Magnetic Circular Dichroism Spectroscopy

  • Brian J. HalesEmail author
Protocol
Part of the Methods in Molecular Biology book series (MIMB, volume 766)

Abstract

Being able to probe the structure and energy levels of metal ions in biological systems is an important goal of bioinorganic scientists. Several of the techniques used rely on the paramagnetic property of certain oxidation states of metal ions. MCD spectroscopy is one of those techniques and represents an effective way of obtaining structure/electronic information of paramagnetic metal ions. The basics of this technique are discussed along with examples of how MCD spectroscopy has been successfully used to elucidate the metal clusters of Nif proteins from nitrogen-fixing bacteria.

Key words

MCD spectroscopy EPR spectroscopy spin–orbit coupling integer spin states paramagnetism zero-field splitting magnetization curves FeMoco P-cluster 

References

  1. 1.
    Piepho SB, Schatz PN (1983) Group Theory in Spectroscopy with Applications to Magnetic Circular Dichroism. Wiley, New York, NYGoogle Scholar
  2. 2.
    Thompson AJ, Cheesman MR, George SJ (1993) Variable-Temperature Magnetic Circular Dichroism. In: Riordan JF, Vallee BL (eds) Metallobiochemistry, Part C, pp. 199–231. Academic, San Diego, CAGoogle Scholar
  3. 3.
    Johnson MK (2000) CD and MCD Spectroscopy. In: Lawrence Que J (ed) Physical Methods in Bioinorganic Chemistry: Spectroscopy and Magnetism, pp. 233–286. University Science Books, Sausalito, CAGoogle Scholar
  4. 4.
    Hagen WR (1992) EPR Spectroscopy of Iron-Sulfur Proteins. In: Sykes AG, Cammack R (eds) Advances in Inorganic Chemistry: Iron-Sulfur Proteins, pp. 165–222. Academic, San Diego, CAGoogle Scholar
  5. 5.
    Lindahl PA, Day EP, Kent TA et al (1985) Mössbauer, EPR, and Magnetization Studies of the Azotobacter vinelandii Fe Protein. J Biol Chem 260:11160–11173PubMedGoogle Scholar
  6. 6.
    Onate YA, Finnegan MG, Hales BJ et al (1993) Variable Temperature Magnetic Circular Dichroism Studies of Reduced Nitrogenase Iron Proteins and [4Fe-4S]+ Synthetic Analog Clusters. Biochim Biophys Acta 1164:113–123PubMedCrossRefGoogle Scholar
  7. 7.
    Palmer G, Multani JS, Cretney WC et al (1972) Electron Paramagnetic Resonance Studies on Nitrogenase—I. The Properties of Molybdoferredoxin and Azoferredoxin. Arch Biochem Biophys 153:325–332PubMedCrossRefGoogle Scholar
  8. 8.
    Johnson MK, Thomson AJ, Robinson AE et al (1981) Characterization of the Paramagnetic Centres of the Molybdenum-Iron Protein of Nitrogenase from Klebsiella pneumoniae Using Low-Temperature Magnetic Circular Dichroism Spectroscopy. Biochim Biophys Acta 671:61–70Google Scholar
  9. 9.
    Kim J, Rees DC (1992) Crystallographic Structure and Functional Implications of the Nitrogenase Molybdenum-Iron Protein from Azotobacter vinelandii. Nature 360:553–560CrossRefGoogle Scholar
  10. 10.
    Hagen WR, Wassink H, Eady RR et al (1987) Quantitative EPR of an S = 7/2 System in Thionine-Oxidized MoFe Proteins of Nitrogenase: A Redefinition on the P-Cluster Concept. Eur J Biochem 169:457–465PubMedCrossRefGoogle Scholar
  11. 11.
    Surerus KK, Hendrich MP, Christie PD et al (1992) Mössbauer and Integer-Spin EPR of the Oxidized P-Clusters of Nitrogenase: Pox Is a Non-Kramers System with a Nearly Degenerate Ground Doublet. J Am Chem Soc 114:8579–8590CrossRefGoogle Scholar
  12. 12.
    Münck E, Rhodes H, Orme-Johnson WH et al (1975) The MoFe Protein Component from Azotobacter vinelandii. Biochim Biophys Acta 400:32–53PubMedGoogle Scholar
  13. 13.
    Broach RB, Rupnik K, Hu Y et al (2004) VTVH-MCD spectroscopic Study of the Metal Clusters in the ΔnifB and ΔnifH MoFe Proteins of Nitrogenase from Azotobacter vinelandii. Biochemistry 45:15039–15048CrossRefGoogle Scholar
  14. 14.
    Lindahl PA, Papaefthymiou V, Orme-Johnson WH et al (1988) Mössbauer Studies of Solid Thionin-Oxidized MoFe Protein of Nitrogenase. J Biol Chem 263:19412–19418PubMedGoogle Scholar

Copyright information

© Springer Science+Business Media, LLC 2011

Authors and Affiliations

  1. 1.Department of ChemistryLouisiana State UniversityBaton RougeUSA

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