Linked Life Data

19655755

Source:http://linkedlifedata.com/resource/pubmed/id/19655755

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
34
pubmed:dateCreated
2009-8-26
pubmed:abstractText
Recently, the conversion of nitrite into NO by certain heme proteins, in particular hemoglobin, gained much interest as a physiologically important source of NO in human tissue. However, in an aqueous environment, nitrite reduction at an iron porphyrin occurs either through oxidation of ferroheme to ferriheme or with the assistance of a second substrate molecule. Here we report on the reduction of nitrite in the absence of a second substrate at the heme center of the ferriheme protein nitrophorin 7 (NP7) resulting in the formation of NO and restoration of the ferriheme center. The product was spectroscopically characterized, in particular by resonance Raman and FT-IR spectroscopy. Performing the reaction in the presence of the NO trap 2-(4-trimethylammonio)phenyl-4,4,5,5-tetramethylimidazoline-1-oxyl 3-oxide (TMA-PTIO) revealed that continuous NO production is possible, i.e., that NP7 is fully restored upon a single turnover. Thus, NP7 is the first case of a b-type heme that performs reduction of nitrite as a single substrate out of the iron(III) state.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1520-5126
pubmed:author
pubmed:issnType
Electronic
pubmed:day
2
pubmed:volume
131
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
12042-3
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Formation of nitric oxide from nitrite by the ferriheme b protein nitrophorin 7.
pubmed:affiliation
Max-Planck-Institut für Bioanorganische Chemie, Stiftstrasse 34-36, D-45470 Mülheim an der Ruhr, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't