Identification of a Novel Bond Between a Histidine and the Essential Tyrosine in Catalase HPII of Escherichia Coli

Overview

Journal Protein Sci

Specialty Biochemistry

Date 1997 May 1

PMID 9144772

Citations 10

Authors

J Bravo

I Fita

J C Ferrer

W Ens

A Hillar

J Switala

P C Loewen

Affiliations

Soon will be listed here.

Abstract

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 sp3 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 degrees 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 H2O2 on the proximal side of the heme with compound 1 is proposed.

Citing Articles

Radical-Mediated Nucleophilic Peptide Cross-Linking in Dynobactin Biosynthesis.

Nguyen B, Gurusinga F, Mettal U, Schaberle T, Yokoyama K J Am Chem Soc. 2024; 146(46):31715-31732.

PMID: 39528355 PMC: 11695099. DOI: 10.1021/jacs.4c10425.

Discovery and biosynthesis of tricyclic copper-binding ribosomal peptides containing histidine-to-butyrine crosslinks.

Li Y, Ma Y, Xia Y, Zhang T, Sun S, Gao J Nat Commun. 2023; 14(1):2944.

PMID: 37221219 PMC: 10206099. DOI: 10.1038/s41467-023-38517-2.

Monofunctional Heme-Catalases.

Hansberg W Antioxidants (Basel). 2022; 11(11).

PMID: 36358546 PMC: 9687031. DOI: 10.3390/antiox11112173.

Deletion of a previously uncharacterized lipoprotein lirL confers resistance to an inhibitor of type II signal peptidase in .

Huang K, Pantua H, Diao J, Skippington E, Volny M, Sandoval W Proc Natl Acad Sci U S A. 2022; 119(38):e2123117119.

PMID: 36099298 PMC: 9499571. DOI: 10.1073/pnas.2123117119.

Formation and Reactivity of New Isoporphyrins: Implications for Understanding the Tyr-His Cross-Link Cofactor Biogenesis in Cytochrome Oxidase.

Ehudin M, Senft L, Franke A, Ivanovic-Burmazovic I, Karlin K J Am Chem Soc. 2019; 141(27):10632-10643.

PMID: 31150209 PMC: 6639807. DOI: 10.1021/jacs.9b01791.

References

Vainshtein B, Barynin V, Vagin A, Grebenko A . Three-dimensional structure of the enzyme catalase. Nature. 1981; 293(5831):411-2. DOI: 10.1038/293411a0. View

Gouet P, Jouve H, Williams P, Andersson I, Andreoletti P, Nussaume L . Ferryl intermediates of catalase captured by time-resolved Weissenberg crystallography and UV-VIS spectroscopy. Nat Struct Biol. 1996; 3(11):951-6. DOI: 10.1038/nsb1196-951. View

Loewen P, Switala J . Purification and characterization of catalase HPII from Escherichia coli K12. Biochem Cell Biol. 1986; 64(7):638-46. DOI: 10.1139/o86-088. View

Mulvey M, Sorby P, Loewen P . Cloning and physical characterization of katE and katF required for catalase HPII expression in Escherichia coli. Gene. 1988; 73(2):337-45. DOI: 10.1016/0378-1119(88)90498-2. View

von Ossowski I, Mulvey M, Leco P, Borys A, Loewen P . Nucleotide sequence of Escherichia coli katE, which encodes catalase HPII. J Bacteriol. 1991; 173(2):514-20. PMC: 207040. DOI: 10.1128/jb.173.2.514-520.1991. View

Jones T, Zou J, Cowan S, Kjeldgaard M . Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A. 1991; 47 ( Pt 2):110-9. DOI: 10.1107/s0108767390010224. View

Stehle T, Ahmed S, Claiborne A, Schulz G . Structure of NADH peroxidase from Streptococcus faecalis 10C1 refined at 2.16 A resolution. J Mol Biol. 1991; 221(4):1325-44. View

Murshudov G, Grebenko A, Barynin V, Vagin A, Vainshtein B, Dauter Z . Three-dimensional structure of catalase from Micrococcus lysodeikticus at 1.5 A resolution. FEBS Lett. 1992; 312(2-3):127-31. DOI: 10.1016/0014-5793(92)80919-8. View

Loewen P, Switala J, von Ossowski I, Hillar A, Christie A, Tattrie B . Catalase HPII of Escherichia coli catalyzes the conversion of protoheme to cis-heme d. Biochemistry. 1993; 32(38):10159-64. DOI: 10.1021/bi00089a035. View

10.

HEIM R, Prasher D, Tsien R . Wavelength mutations and posttranslational autoxidation of green fluorescent protein. Proc Natl Acad Sci U S A. 1994; 91(26):12501-4. PMC: 45466. DOI: 10.1073/pnas.91.26.12501. View

11.

Gouet P, Jouve H, Dideberg O . Crystal structure of Proteus mirabilis PR catalase with and without bound NADPH. J Mol Biol. 1995; 249(5):933-54. DOI: 10.1006/jmbi.1995.0350. View

12.

Bravo J, Verdaguer N, Tormo J, Betzel C, Switala J, Loewen P . Crystal structure of catalase HPII from Escherichia coli. Structure. 1995; 3(5):491-502. DOI: 10.1016/s0969-2126(01)00182-4. View

13.

Cubitt A, HEIM R, Adams S, Boyd A, Gross L, Tsien R . Understanding, improving and using green fluorescent proteins. Trends Biochem Sci. 1995; 20(11):448-55. DOI: 10.1016/s0968-0004(00)89099-4. View

14.

Murshudov G, Grebenko A, Barynin V, Dauter Z, Wilson K, Vainshtein B . Structure of the heme d of Penicillium vitale and Escherichia coli catalases. J Biol Chem. 1996; 271(15):8863-8. DOI: 10.1074/jbc.271.15.8863. View

15.

Murthy M, Reid 3rd T, Sicignano A, Tanaka N, Rossmann M . Structure of beef liver catalase. J Mol Biol. 1981; 152(2):465-99. DOI: 10.1016/0022-2836(81)90254-0. View