Retracted Article: On the enzymatic activity of catalase: an iron L-edge X-ray absorption study of the active centre

Nora Bergmann; Sébastien Bonhommeau; Kathrin M. Lange; Stefanie M. Greil; Stefan Eisebitt; Frank de Groot; Majed Chergui; Emad F. Aziz

doi:10.1039/B924245G

Retracted Article: On the enzymatic activity of catalase: an iron L-edge X-ray absorption study of the active centre†

Nora Bergmann,^a Sébastien Bonhommeau,^b Kathrin M. Lange,^c Stefanie M. Greil,^c Stefan Eisebitt,^cd Frank de Groot,^e Majed Chergui*^f and Emad F. Aziz*^cf

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* Corresponding authors

^a Max-Delbrück-Center for Molecular Medicine, D-13125 Berlin-Buch, Germany

^b Institut des Sciences Moléculaires-UMR 5255 CNRS, Université Bordeaux 1, 351 cours de la Libération, 33405 Talence Cedex, France

^c Helmholtz-Zentrum Berlin für Materialen und Energie c/o BESSY II, Albert-Einstein Strasse 15, 12489 Berlin, Germany
E-mail: Emad.Aziz@helmholtz-berlin.de

^d Technical University Berlin, Institute for Optics and Atomic Physics ER 1-1 Strasse des 17. Juni 135, 10623 Berlin, Germany

^e Department of Inorganic Chemistry and Catalysis, Sorbonnelaan 16, 3584 CA Utrecht, The Netherlands

^f Ecole Polytechnique Fédérale de Lausanne, Laboratoire de Spectroscopie Ultrarapide, Faculté des Sciences de Base, ISIC-BSP, CH-1015 Lausanne-Dorigny, Switzerland
E-mail: Majed.Chergui@epfl.ch

Abstract

Catalase and methaemoglobin have very similar haem groups, which are both ferric, yet catalase decomposes hydrogen peroxide to water and oxygen very efficiently, while methaemoglobin does not. Structural studies have attributed this behaviour to their different distal environments. Here we present Fe L_2,3-edge X-ray absorption spectra of these proteins in physiological solutions, which reveal clear differences in their electronic structures, in that π back-donation of the Fe atom occurs in catalase, which confers on it a partial ferryl (Fe⁴⁺) character, while this is not the case in methaemoglobin. The origin of the Fe⁴⁺ character stems from the proximal tyrosine residue. We also find that both systems are in a high spin state. Temperature effects influence the spectra of catalase only weakly, in agreement with previous studies of its chemical activity. We conclude that the high activity of catalase is not only determined by its distal environment but also by its partial ferryl character.

Physical Chemistry Chemical Physics

Retracted Article: On the enzymatic activity of catalase: an iron L-edge X-ray absorption study of the active centre†

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