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NMR Approaches to the Study of Structure-Function Relationships in Iron-Sulfur Proteins

Rubredoxin, [2Fe-2s] Ferredoxins, and a Rieske Protein

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Protein Structure — Function Relationship

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Abstract

Newer NMR methods, particularly in conjunction with stable isotope labeling (with 2H, 13C, and 15N), offer powerful approaches to the elucidation of structure-function relationships in paramagnetic proteins such as iron-sulfur proteins. The optimization ofNMR pulse sequences for rapidly-relaxing spins and the utilization of multidimensional multinuclear NMR spectroscopy have made it possible to determine sequence-specific assignments for a large number of NMR signals in rubredoxins, ferredoxins, and high-potential iron proteins, including some from the cysteine residues that ligate the iron ions. Such assignments are the key to a wealth of information derived from NMR parameters, such as the temperature and pH dependence of chemical shifts and the relaxation properties of the resonances that report on interactions between nuclei of the protein and unpaired electron density from the metal center. This information can be used to test theoretical descriptions of electron distribution within these molecules and to model the structures and dynamic properties of the proteins in solution. Mutagenesis of these proteins, followed by biochemical evaluation of their functional properties and biophysical analysis of their structures and stabilities, is beginning to reveal which residues are important for cluster formation and which residues play a role in electron transfer to and from redox partner proteins. This review discusses recent NMR studies from our laboratory of six iron-sulfur proteins: Clostridium pasteurianum rubredoxin, the vegetative and heterocyst ferredoxins from Anabaena 7120, human ferredoxin, and the Pseudomonas mendocina KR1 tmoC Rieske protein.

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  1. Hong Cheng

    Present address: Mayo Research Institute, Rochester, Minnesota, USA

Authors and Affiliations

  1. Department of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin, 53706, USA

    John L. Markley, Bin **a, Young Kee Chae, Hong Cheng & William M. Westler

  2. Institute for Enzyme Research, University of Wisconsin-Madison, Madison, Wisconsin, 53706, USA

    Jeremie D. Pikus & Brian G. Fox

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  1. John L. Markley
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  4. Hong Cheng
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Editors and Affiliations

  1. H. E. J. Research Institute of Chemistry, University of Karachi, Karachi, Pakistan

    Zafar H. Zaidi

  2. Department of Chemistry, University of Nebraska, Lincoln, Nebraska, USA

    David L. Smith

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© 1996 Plenum Press, New York

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Markley, J.L. et al. (1996). NMR Approaches to the Study of Structure-Function Relationships in Iron-Sulfur Proteins. In: Zaidi, Z.H., Smith, D.L. (eds) Protein Structure — Function Relationship. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-0359-6_14

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