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Chemical modification of hemoglobin improves biocatalytic oxidation of PAHs.

Abstract：

:Chemical modifications on human hemoglobin were performed with the aim to change both surface and active-site hydrophobicities. The modifications included covalent coupling of poly(ethylene)glycol (5000 MW) on free amino groups and the methyl esterification of free carboxylic groups. The modified hemoglobin was assayed for the oxidation of 11 polycyclic aromatic hydrocarbons (PAHs) and 2 organosulfur aromatic compounds. Acenaphthene, anthracene, azulene, benzo(a)pyrene, fluoranthene, fluorene, phenanthrene, and pyrene were transformed to their respective quinones, while for chrysene and biphenyl no biocatalytic reaction could be detected. Dibenzothiophene and thianthrene were oxidized to form sulfoxides. The doubly modified hemoglobin, PEG-Met-hemoglobin, showed up to 10 times higher activity than the unmodified protein. The kinetic constants show that the PEG-Met-hemoglobin has a significantly higher catalytic efficiency. The equilibrium substrate binding constants for unmodified and PEG-Met-modified hemoglobis and hemoglobin show that this catalytic enhancement could be attributed to the affinity increase for hydrophobic substrates in the modified protein.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Torres E,Vazquez-Duhalt R

doi

10.1006/bbrc.2000.3016

subject

Has Abstract

pub_date

2000-07-14 00:00:00

pages

820-3

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(00)93016-X

journal_volume

273

pub_type

杂志文章

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