Linked Life Data

19606432

Source:http://linkedlifedata.com/resource/pubmed/id/19606432

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
2009-10-21
pubmed:abstractText
Hemoglobin is a member of the hemoprotein superfamily whose main role is to transport O(2) in vertebrate organisms. It has two known promiscuous enzymatic activities, peroxidase and oxygenase. Here we show for the first time that bovine hemoglobin also presents a catalase-like activity characterized by a V(max )of 344 microM/min, a K(M )of 24 mM and a k(cat) equal to 115/min. For high anthracene and hemoglobin concentrations and low hydrogen peroxide concentrations, this activity inhibits the expected oxidation of anthracene, which occurs through a peroxidase-like mechanism. Anthracene belongs to the polycyclic aromatic hydrocarbon (PAH) family whose members are carcinogenic and persistent pollutants found in industrial waste waters. Our results show that anthracene oxidation by hemoglobin and hydrogen peroxide follows a typical bi-bi ping-pong mechanism with a V(max) equal to 0.250 microM/min, K(M(H2O2) )of 80 microM, K(M(ANT)) of 1.1 microM and k(cat) of 0.17/min. The oxidation of anthracene is shown to be pseudo-catalytic because an excess of hemoglobin and hydrogen peroxide is required to make PAH completely disappear. Thus, bovine hemoglobin presents, in different degrees, all the catalytic activities of the hemoprotein group, which makes it a very interesting protein for biotechnological processes and one with which structure-activity relationships can be studied.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1860-7314
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
4
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1460-70
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Catalase-like activity of bovine met-hemoglobin: interaction with the pseudo-catalytic peroxidation of anthracene traces in aqueous medium.
pubmed:affiliation
Institut Charles Gerhardt Montpellier, Equipe des Matériaux Avancés pour la Catalyse et la Santé, UMR 5253 CNRS/ENSCM/UM2/UM1, 34296 Montpellier, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't