TY  - GEN
AB  - This study investigates mechanisms by which metalloproteins reduce nitric oxide (NO) to nitrous oxide (N₂O), a key step in bacterial denitrification and nitrosative stress resistance. Using spectroscopic techniques, we show that NO binds first to heme iron(II) in terminal oxidases and engineered NOR models, while distal metals stabilize a heme-hyponitrite intermediate rather than directly binding NO. Flavodiiron proteins (FDPs) were also examined; deflavo-FDP retained single-turnover NO reduction, indicating the diiron center catalyzes NO reduction while FMN regenerates the oxidized site. These findings reveal distinct catalytic routes and roles of metal centers in NO reductase activity.
AD  - Oregon Health and Science University
AU  - Hayashi, Takahiro
DA  - 2011
DO  - 10.6083/M4G44N8H
DO  - DOI
ED  - Moënne-Loccoz, Pierre
ED  - Advisor
ID  - 599
KW  - Spectrum Analysis
KW  - Denitrification
KW  - Oxidoreductases
KW  - Iron Compounds
KW  - Nitric Oxide
KW  - Nitric Oxide Synthase
KW  - Fourier Analysis
KW  - Spectrum Analysis, Raman
KW  - raman spectroscopy
KW  - diiron
L1  - https://digitalcollections.ohsu.edu/record/599/files/600_etd.pdf
L2  - https://digitalcollections.ohsu.edu/record/599/files/600_etd.pdf
L4  - https://digitalcollections.ohsu.edu/record/599/files/600_etd.pdf
LK  - https://digitalcollections.ohsu.edu/record/599/files/600_etd.pdf
N2  - This study investigates mechanisms by which metalloproteins reduce nitric oxide (NO) to nitrous oxide (N₂O), a key step in bacterial denitrification and nitrosative stress resistance. Using spectroscopic techniques, we show that NO binds first to heme iron(II) in terminal oxidases and engineered NOR models, while distal metals stabilize a heme-hyponitrite intermediate rather than directly binding NO. Flavodiiron proteins (FDPs) were also examined; deflavo-FDP retained single-turnover NO reduction, indicating the diiron center catalyzes NO reduction while FMN regenerates the oxidized site. These findings reveal distinct catalytic routes and roles of metal centers in NO reductase activity.
PB  - Oregon Health and Science University
PY  - 2011
T1  - Mechanistic studies of NO reduction in dinuclear metalloproteins
TI  - Mechanistic studies of NO reduction in dinuclear metalloproteins
UR  - https://digitalcollections.ohsu.edu/record/599/files/600_etd.pdf
Y1  - 2011
ER  -