TY - JOUR
T1 - Lewis Acid Activation of the Ferrous Heme-NO Fragment toward the N-N Coupling Reaction with NO to Generate N2O
AU - Abucayon, Erwin G.
AU - Khade, Rahul L.
AU - Powell, Douglas R.
AU - Zhang, Yong
AU - Richter-Addo, George B.
N1 - Publisher Copyright:
© 2018 American Chemical Society.
PY - 2018/3/28
Y1 - 2018/3/28
N2 - Bacterial NO reductase (bacNOR) enzymes utilize a heme/non-heme active site to couple two NO molecules to N2O. We show that BF3 coordination to the nitrosyl O-atom in (OEP)Fe(NO) activates it toward N-N bond formation with NO to generate N2O. 15N-isotopic labeling reveals a reversible nitrosyl exchange reaction and follow-up N-O bond cleavage in the N2O formation step. Other Lewis acids (B(C6F5)3 and K+) also promote the NO coupling reaction with (OEP)Fe(NO). These results, complemented by DFT calculations, provide experimental support for the cis:b3 pathway in bacNOR.
AB - Bacterial NO reductase (bacNOR) enzymes utilize a heme/non-heme active site to couple two NO molecules to N2O. We show that BF3 coordination to the nitrosyl O-atom in (OEP)Fe(NO) activates it toward N-N bond formation with NO to generate N2O. 15N-isotopic labeling reveals a reversible nitrosyl exchange reaction and follow-up N-O bond cleavage in the N2O formation step. Other Lewis acids (B(C6F5)3 and K+) also promote the NO coupling reaction with (OEP)Fe(NO). These results, complemented by DFT calculations, provide experimental support for the cis:b3 pathway in bacNOR.
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U2 - 10.1021/jacs.7b13681
DO - 10.1021/jacs.7b13681
M3 - Article
C2 - 29502400
AN - SCOPUS:85044676475
SN - 0002-7863
VL - 140
SP - 4204
EP - 4207
JO - Journal of the American Chemical Society
JF - Journal of the American Chemical Society
IS - 12
ER -