Protein Science, Vol 6, Issue 5 1016-1023, Copyright © 1997 by Cold Spring Harbor Laboratory Press

ARTICLE

Identification of a novel bond between a histidine and the essential tyrosine in catalase HPII of Escherichia coli

J. BRAVO, I. FITA, J. C. FERRER, W. ENS, A. HILLAR, J. SWITALA and P. C. LOEWEN
Centro de Investigacion y Desarrollo (C.S.I.C.), Jordi Girona Salgado 18-26, 08034 Barcelona, Spain Present address: Laboratory of Molecular Biophysics, The Rex Richards Building, South Parks Road, Oxford OX1 3OU, United Kingdom.

A bond between the N({delta}) of the imidazole ring of His 392 and the C({beta}) of the essential Tyr 415 has been found in the refined crystal structure at 1.9 A resolution of catalase HPII of Escherichia coli. This novel type of covalent linkage is clearly defined in the electron density map of HPII and is confirmed by matrix-assisted laser desorption/ionization mass spectrometry analysis of tryptic digest mixtures. The geometry of the bond is compatible with both the sp(3) hybridization of the C({beta}) atom and the planarity of the imidazole ring. Two mutated variants of HPII active site residues, H128N and N201H, do not contain the His 392-Tyr 415 bond, and their crystal structures show that the imidazole ring of His 392 was rotated, in both cases, by 80{deg} relative to its position in HPII. These mutant forms of HPII are catalytically inactive and do not convert heme b to heme d, suggesting a relationship between the self-catalyzed heme conversion reaction and the formation of the His-Tyr linkage. A model coupling the two processes and involving the reaction of one molecule of H(2)O(2) on the proximal side of the heme with compound I is proposed.
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