Linked Life Data

19580299

Source:http://linkedlifedata.com/resource/pubmed/id/19580299

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
15
pubmed:dateCreated
2009-9-2
pubmed:abstractText
Hydrogenases comprise a variety of enzymes that catalyze the reversible oxidation of molecular hydrogen. Out of this group, [FeFe]-hydrogenase shows the highest activity for hydrogen production which is, therefore, of great interest in the field of renewable energies. Unfortunately, this comes with the flaw of a generally very high sensitivity against molecular oxygen that irreversibly inhibits this enzyme. While many studies have already addressed the mechanism of hydrogen formation by [FeFe]-hydrogenase, little is known about the molecular and mechanistic details leading to enzyme inactivation by O(2). In order to elucidate this process, we performed density functional theory calculations on several possible O(2) adducts of the catalytic center--the so-called H-cluster--and show that the direct interaction of the [2Fe](H) subsite with dioxygen is an exothermic and specific reaction in which O(2) most favorably binds in an end-on manner to the distal Fe(d). Based on the results, we propose a protonation mechanism that can explain the irreversibility of dioxygen-induced enzyme inactivation by water release and degradation of the ligand environment of the H-cluster.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1520-510X
pubmed:author
pubmed:issnType
Electronic
pubmed:day
3
pubmed:volume
48
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7127-40
pubmed:dateRevised
2010-9-27
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Theoretical study of dioxygen induced inhibition of [FeFe]-hydrogenase.
pubmed:affiliation
Laboratorium für Physikalische Chemie, ETH Zurich, Wolfgang-Pauli-Strasse 10 8093 Zürich, Switzerland.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't