| Issue |
J. Phys. IV France
Volume 7, Number C2, Avril 1997
Proceedings of the 9th International Conference on X-Ray Absorption Fine Structure
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| Page(s) | C2-611 - C2-614 | |
| DOI | https://doi.org/10.1051/jp4/1997113 | |
J. Phys. IV France 7 (1997) C2-611-C2-614
DOI: 10.1051/jp4/1997113
Difference EXAFS Studies of Nitrogenase and Nitrite Reductase Enzymes of the Nitrogen Cycle
R. R. Eady1, B. E. Smith1, Z. H. L. Abraham1, F. E. Dodd2, 3, J. G. Grossmann3, L. M. Murphy3, R. W. Strange3 and S. S. Hasnain31 Nitrogen Fixation Laboratory, John Innes Centre, Colney, Norwich NR4 7UH, UK
2 DeMontfort University, Leicester LEI 9BH, UK
3 CCLRC Daresbury Laboratory, Warrington WA4 4AD, UK
Abstract
Difference EXAFS can be exploited to take full advantage of the power of the EXAFS technique in providing
high resolution metrical information around the active centres of metalloenzymes during turnover and/or the binding of
substrates or inhibitors. Difference EXAFS data are presented for (a) the Mo-nitrogenase of Klebsiella pneumoniae (Fe and
Mo K-edges), under conditions of enzyme turnover designed to maximize the concentration of species of the MoFe protein
containing reduced FeMoco, (b) the copper-containing dissimilatory nitrite reductase of Alcaligenes xylosoxidans. In this
case, difference EXAFS data provide direct structure/function relationships for changes associated with binding of substrate
to the oxidized enzyme and also the reduction of the enzyme.
© EDP Sciences 1997