|
Accession number;04A0258624
|
| Title;Structural and Electronic Characterization of Reaction Intermediate of Nitric Oxide Reductase from Pseudomonas aeruginosa. |
| Author;
|
Journal Title;Abstracts. Symposium on Biofunctional Chemistry
|
Journal Code:L0836A
|
ISSN:
|
|
VOL.18th;NO.;PAGE.84-85(2003)
|
| Figure&Table&Reference;FIG.2 |
| Pub. Country;Japan |
| Language;Japanese |
| Abstract;The reaction intermediate in the single turnover of NO reduction by NO reductase (NOR) from Pseudomonas aeruginosa was characterized by the time-resolved EPR spectroscopy combined with the originally designed freeze-quench device. In the EPR spectrum of the 0.5 ms quenched sample, two characteristic signals of g=4.0 and g-2 with three lines of the hyperfine splitting by the bound 14NO are observed. The former is derived from the non-heme Fe2+-NO complex with S=3/2 state, and the latter form the penta-coordinated nitrocyl-heme iron. In the reaction intermediate, two NO molecules bind to each metal center of the catalytic site for formation of the FeB-NO and nitrocyl-heme b3 complexes. In the nitrocyl-heme b3 site, the proximal histidine is dissociated. (author abst.) |
|
|
|
Related Articles;
|
