The preparation and characterization of a new microperoxidase obtained from proteinase K-treated cytochrome (C552) from Marinobacter hydrocarbonoclasticus (previously known as Pseudomonas nautica) are presented. This microperoxidase (MMP-5) has novel structural properties relative to previously reported microperoxidases, as the two intervening amino acid (X) residues within the consensual CXXCH c-type heme binding motif are missing, yielding a heme-pentapeptide with increased solubility in aqueous solvents and a 1-2 order of magnitude higher stability of the monomeric state relative to canonical microperoxidases. The electronic spectra in the near-UV and visible regions have been studied as a function of MMP-5 concentration and pH. The spectroscopic properties of MMP-5 are typical of microperoxidases with high-spin hexa- or pentacoordinate heme species dominant in the 1-8 pH range and low-spin states prevailing at higher pH values. In the presence of hydrogen peroxide, MMP-5 displays peroxidatic activities towards several compounds. (c) 2005 Elsevier B.V. All rights reserved.
A new microperoxidase from Marinobacter hydrocarbonoclasticus / Lorenzo, Caputi; Alessandra Di, Tullio; Luana Di, Leandro; Francesco De, Angelis; Malatesta, Francesco. - In: BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS. - ISSN 0304-4165. - STAMPA. - 1725:1(2005), pp. 71-80. [10.1016/j.bbagen.2005.05.023]
A new microperoxidase from Marinobacter hydrocarbonoclasticus
MALATESTA, FRANCESCO
2005
Abstract
The preparation and characterization of a new microperoxidase obtained from proteinase K-treated cytochrome (C552) from Marinobacter hydrocarbonoclasticus (previously known as Pseudomonas nautica) are presented. This microperoxidase (MMP-5) has novel structural properties relative to previously reported microperoxidases, as the two intervening amino acid (X) residues within the consensual CXXCH c-type heme binding motif are missing, yielding a heme-pentapeptide with increased solubility in aqueous solvents and a 1-2 order of magnitude higher stability of the monomeric state relative to canonical microperoxidases. The electronic spectra in the near-UV and visible regions have been studied as a function of MMP-5 concentration and pH. The spectroscopic properties of MMP-5 are typical of microperoxidases with high-spin hexa- or pentacoordinate heme species dominant in the 1-8 pH range and low-spin states prevailing at higher pH values. In the presence of hydrogen peroxide, MMP-5 displays peroxidatic activities towards several compounds. (c) 2005 Elsevier B.V. All rights reserved.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
