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Pierre Moënne-Loccoz

Researcher at Oregon Health & Science University

Publications -  140
Citations -  5425

Pierre Moënne-Loccoz is an academic researcher from Oregon Health & Science University. The author has contributed to research in topics: Heme & Ligand. The author has an hindex of 40, co-authored 131 publications receiving 4952 citations. Previous affiliations of Pierre Moënne-Loccoz include University of Rhode Island & University of Oregon.

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Nitric Oxide in Biological Denitrification: Fe/Cu Metalloenzyme and Metal Complex NOx Redox Chemistry

TL;DR: This paper aims to demonstrate the efforts towards in-situ applicability of EMMARM, which aims to provide real-time information about the “building blocks” of EMT and its role in disease.
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O2 Activation by Non-Heme Diiron Proteins: Identification of a Symmetric μ-1,2-Peroxide in a Mutant of Ribonucleotide Reductase†

TL;DR: The first definitive evidence for a bridging, symmetrical peroxo adduct is presented from vibrational spectroscopic studies of the freeze-trapped intermediate of this mutant R2.
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The ferroxidase reaction of ferritin reveals a diferric μ-1,2 bridging peroxide intermediate in common with other O2-activating non-heme diiron proteins

TL;DR: To characterize this transient intermediate and establish unambiguously the peroxodiferric assignment, rapid freeze-quenching was used to trap the initial intermediate for resonance Raman investigation, andrete vibrational modes are observed for this intermediate, indicating a single chromophore in a homogeneous state, in agreement with the Mössbauer conclusions.
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Roles of the proximal heme thiolate ligand in cytochrome p450(cam).

TL;DR: These experiments confirm that the thiolate ligand facilitates the O--O bond cleavage by P450 enzymes and also demonstrate that this ligand satisfies important roles in protein folding, substrate binding, and electron transfer.
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Heme Oxygenase-1, Intermediates in Verdoheme Formation and the Requirement for Reduction Equivalents

TL;DR: Conversion of heme to verdoheme by heme oxygenase-1 (HO-1) is thought to involve α-meso-hydroxylation and elimination of the meso-carbon as CO, a reaction supported by both H2O2 and NADPH-cytochrome P450 reductase/O2.