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Jeffrey Harmer

Researcher at University of Queensland

Publications -  120
Citations -  3886

Jeffrey Harmer is an academic researcher from University of Queensland. The author has contributed to research in topics: Electron paramagnetic resonance & Pulsed EPR. The author has an hindex of 36, co-authored 109 publications receiving 3329 citations. Previous affiliations of Jeffrey Harmer include University of Basel & Max Planck Society.

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How Escherichia coli Is Equipped to Oxidize Hydrogen under Different Redox Conditions

TL;DR: The enterobacterium Escherichia coli synthesizes two H2 uptake enzymes, Hyd-1 and Hyd-2, which are well suited for fast and efficient catalysis in more reducing environments, and may be individually optimized to function under distinct environmental conditions.
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Size dependent oxygen buffering capacity of ceria nanocrystals

TL;DR: The structural, chemical and electronic changes of ceria as a function of decreasing particle size have been studied: at sizes below 5 nm the total amount of reducible oxygen dramatically increases due to superoxide formation on the ceria surface, a result indicative of a size dependent oxygen buffering capacity.
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A stable aminyl radical metal complex

TL;DR: It is reported that transition metal coordination also supports an aminyl radical, resulting in a stable crystalline complex: [Rh(I)(trop2N.)(bipy)]+OTf–, which supports 57% localization of the unpaired spin at N.
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Sodium phosphaethynolate, Na(OCP), as a “P” transfer reagent for the synthesis of N-heterocyclic carbene supported P3 and PAsP radicals

TL;DR: In this paper, the electron transfer was used to reveal the central pnictogen atom in both cases as the main carrier of the spin density (∼60%), and that they are best described as the P3 or PAsP analogues of the elusive allyl radical dianion.
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Direct assignment of EPR spectra to structurally defined iron-sulfur clusters in complex I by double electron–electron resonance

TL;DR: Double electron-electron resonance (DEER) spectroscopy on B. taurus complex I with the structure of the hydrophilic domain of Thermus thermophilus complex I combines the magnetic moments of the clusters and the orientation selectivity of the DEER experiment explicitly to assign signal N4 to the first 4Fe cluster in the TYKY subunit, and N5 to the all-cysteine ligated 4Fe clusters in the 75 kDa subunit.