Autocatalytic formation of green heme: evidence for H2O2-dependent formation of a covalent methionine-heme linkage in ascorbate peroxidase.

Journal article

The mammalian heme peroxidases are distinguished from their plant and fungal counterparts by the fact that the heme group is covalently bound to the protein through ester links from glutamate and aspartate residues to the heme 1- and 5-methyl groups and, in the case of myeloperoxidase, through an additional sulfonium link from the Cbeta of the 2-vinyl group to a methionine residue. To duplicate the sulfonium link in myeloperoxidase and to obtain information on its mechanism of formation, we h...

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Authors: Metcalfe, C; Ott, M; Patel, N; Singh, K; Mistry, S

• Publication status: Published
• Journal: Journal of the American Chemical Society
• Volume: 126
• Issue: 49
• Pages: 16242-16248
• Publication date: 2004-12-01
• DOI: 10.1021/ja048242c
• EISSN: 1520-5126
• ISSN: 0002-7863
• Language: English
• Keywords: Spectrophotometry, Ultraviolet; Plant Proteins; Kinetics; Peroxidases; Methionine; Amino Acid Sequence; Peas; Molecular Sequence Data; Hydrogen Peroxide; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Models, Molecular; Mutagenesis, Site-Directed; Heme; Ascorbate Peroxidases; Recombinant Proteins; Catalysis