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Structural studies of Proteus mirabilis catalase in its ground state, oxidized state and in complex with formic acid.

Andreoletti P, Pernoud A, Sainz G, Gouet P, Jouve HM
Acta Crystallogr D Biol Crystallogr 59 2163-8 (2003)
Cited: 7 times
EuropePMC logo PMID: 14646074

Abstract

The structure of Proteus mirabilis catalase in complex with an inhibitor, formic acid, has been solved at 2.3 A resolution. Formic acid is a key ligand of catalase because of its ability to react with the ferric enzyme, giving a high-spin iron complex. Alternatively, it can react with two transient oxidized intermediates of the enzymatic mechanism, compounds I and II. In this work, the structures of native P. mirabilis catalase (PMC) and compound I have also been determined at high resolution (2.0 and 2.5 A, respectively) from frozen crystals. Comparisons between these three PMC structures show that a water molecule present at a distance of 3.5 A from the haem iron in the resting state is absent in the formic acid complex, but reappears in compound I. In addition, movements of solvent molecules are observed during formation of compound I in a cavity located away from the active site, in which a glycerol molecule is replaced by a sulfate. These results give structural insights into the movement of solvent molecules, which may be important in the enzymatic reaction.

Reviews - 1mqf mentioned but not cited (1)

  1. Monofunctional Heme-Catalases. Hansberg W. Antioxidants (Basel) 11 2173 (2022)

Articles - 1mqf mentioned but not cited (2)

  1. Local Electric Fields as a Natural Switch of Heme-Iron Protein Reactivity. Bím D, Alexandrova AN. ACS Catal 11 6534-6546 (2021)
  2. An Algorithm for Computing Side Chain Conformational Variations of a Protein Tunnel/Channel. Seo U, Kim KJ, Kang BS. Molecules 23 E2459 (2018)


Reviews citing this publication (2)

  1. Classical catalase: ancient and modern. Nicholls P. Arch. Biochem. Biophys. 525 95-101 (2012)
  2. The influence of X-rays on the structural studies of peroxide-derived myoglobin intermediates. Hersleth HP, Hsiao YW, Ryde U, Görbitz CH, Andersson KK. Chem. Biodivers. 5 2067-2089 (2008)

Articles citing this publication (2)

  1. Spectroscopic description of an unusual protonated ferryl species in the catalase from Proteus mirabilis and density functional theory calculations on related models. Consequences for the ferryl protonation state in catalase, peroxidase and chloroperoxidase. Horner O, Mouesca JM, Solari PL, Orio M, Oddou JL, Bonville P, Jouve HM. J. Biol. Inorg. Chem. 12 509-525 (2007)
  2. Purification, cloning, expression, and biochemical characterization of a monofunctional catalase, KatP, from Pigmentiphaga sp. DL-8. Dong W, Hou Y, Li S, Wang F, Zhou J, Li Z, Wang Y, Huang F, Fu L, Huang Y, Cui Z. Protein Expr. Purif. 108 54-61 (2015)


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