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Methods in Molecular Biology (Clifton, N.J.)|March 19, 2014
Characterizing millisecond intermediates in hemoproteins using rapid-freeze-quench resonance Raman spectroscopyHirotoshi Matsumura, Pierre Moënne-Loccoz
Journal of the American Chemical Society|September 13, 2022
Spectroscopic Characterization of a Diferric Mycobacterial Hemerythrin-Like Protein with Unprecedented Reactivity toward Nitric OxideTherese Albert, Pierre Moënne-Loccoz
Journal of Inorganic Biochemistry|June 9, 2024
Vibrational analyses of the reaction of oxymyoglobin with NO using a photolabile caged NO donor at cryogenic temperaturesTherese Albert, Arun Kumar, Jonathan Caranto, et al.
Journal of the American Chemical Society|November 26, 2004
Two CO molecules can bind concomitantly at the diiron site of NO reductase from Bacillus azotoformansShen Lu, Suharti, Simon de Vries, et al.
Proceedings of the National Academy of Sciences of the United States of America|May 4, 2022
Distinct roles of the Na+ binding sites in the allosteric coupling mechanism of the glutamate transporter homolog, GltPhErika A Riederer, Pierre Moënne-Loccoz, Francis I Valiyaveetil
Journal of the American Chemical Society|May 28, 2009
The millisecond intermediate in the reaction of nitric oxide with oxymyoglobin is an iron(III)--nitrato complex, not a peroxynitriteErik T Yukl, Simon de Vries, Pierre Moënne-Loccoz
Inorganic Chemistry|December 9, 2022
Influence of the Interdomain Interface on Structural and Redox Properties of Multiheme ProteinsFangfang Zhong, Therese Albert, Pierre Moënne-Loccoz, et al.
Journal of the American Chemical Society|December 5, 2018
Nitric Oxide Reductase Activity in Heme-Nonheme Binuclear Engineered Myoglobins through a One-Electron Reduction CycleSinan Sabuncu, Julian H Reed, Yi Lu, et al.
Journal of the American Chemical Society|January 18, 2014
The production of nitrous oxide by the heme/nonheme diiron center of engineered myoglobins (Fe(B)Mbs) proceeds through a trans-iron-nitrosyl dimerHirotoshi Matsumura, Takahiro Hayashi, Saumen Chakraborty, et al.
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