A new microperoxidase from Marinobacter hydrocarbonoclasticus.
The preparation and characterization of a new microperoxidase obtained from proteinase K-treated cytochrome c(552) 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.
Department of Pure and Applied Biology, University of L'Aquila, L'Aquila, Italy.
Lorenzo
L
Caputi
Alessandra
A
Di Tullio
Luana
L
Di Leandro
Francesco
F
De Angelis
Francesco
F
Malatesta
D034241:Alteromonadaceae / Q000201:enzymology*; D000595:Amino Acid Sequence; D003574:Cytochrome c Group / Q000737:chemistry / Q000378:metabolism; D006861:Hydrogen Peroxide / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D008024:Ligands; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010544:Peroxidases / Q000737:chemistry* / Q000378:metabolism*; D011485:Protein Binding
D003574:Cytochrome c Group; D008024:Ligands; C022302:cytochrome C-552; D006861:Hydrogen Peroxide; D010544:Peroxidases; C021799:microperoxidase