The spectroscopy of nitrogenases

C Van Stappen, L Decamps, GE Cutsail III… - Chemical …, 2020 - ACS Publications
Nitrogenases are responsible for biological nitrogen fixation, a crucial step in the
biogeochemical nitrogen cycle. These enzymes utilize a two-component protein system and …

Particulate methane monooxygenase contains only mononuclear copper centers

MO Ross, F MacMillan, J Wang, A Nisthal, TJ Lawton… - Science, 2019 - science.org
Bacteria that oxidize methane to methanol are central to mitigating emissions of methane, a
potent greenhouse gas. The nature of the copper active site in the primary metabolic …

Product analogue binding identifies the copper active site of particulate methane monooxygenase

FJ Tucci, RJ Jodts, BM Hoffman, AC Rosenzweig - Nature Catalysis, 2023 - nature.com
Nature's primary methane-oxidizing enzyme, the membrane-bound particulate methane
monooxygenase (pMMO), catalyses the oxidation of methane to methanol. Copper is …

Cobalt–carbon bonding in a salen-supported cobalt (IV) alkyl complex postulated in oxidative MHAT catalysis

CV Wilson, D Kim, A Sharma, RX Hooper… - Journal of the …, 2022 - ACS Publications
The catalytic hydrofunctionalization of alkenes through radical-polar crossover metal
hydrogen atom transfer (MHAT) offers a mild pathway for the introduction of functional …

[HTML][HTML] Advanced paramagnetic resonance spectroscopies of iron–sulfur proteins: Electron nuclear double resonance (ENDOR) and electron spin echo envelope …

GE Cutsail III, J Telser, BM Hoffman - Biochimica et Biophysica Acta (BBA) …, 2015 - Elsevier
The advanced electron paramagnetic resonance (EPR) techniques, electron nuclear double
resonance (ENDOR) and electron spin echo envelope modulation (ESEEM) spectroscopies …

Characterization of an FeN–NH2 Intermediate Relevant to Catalytic N2 Reduction to NH3

JS Anderson, GE Cutsail III, J Rittle… - Journal of the …, 2015 - ACS Publications
The ability of certain transition metals to mediate the reduction of N2 to NH3 has attracted
broad interest in the biological and inorganic chemistry communities. Early transition metals …

Coordination of the Copper Centers in Particulate Methane Monooxygenase: Comparison between Methanotrophs and Characterization of the CuC Site by EPR and …

RJ Jodts, MO Ross, CW Koo, PE Doan… - Journal of the …, 2021 - ACS Publications
In nature, methane is oxidized to methanol by two enzymes, the iron-dependent soluble
methane monooxygenase (sMMO) and the copper-dependent particulate MMO (pMMO) …

13C ENDOR Characterization of the Central Carbon within the Nitrogenase Catalytic Cofactor Indicates That the CFe6 Core Is a Stabilizing “Heart of Steel”

DA Lukoyanov, ZY Yang… - Journal of the …, 2022 - ACS Publications
Substrates and inhibitors of Mo-dependent nitrogenase bind and react at Fe ions of the
active-site FeMo-cofactor [7Fe–9S–C–Mo–homocitrate] contained within the MoFe protein α …

High-Resolution ENDOR Spectroscopy Combined with Quantum Chemical Calculations Reveals the Structure of Nitrogenase Janus Intermediate E4(4H)

V Hoeke, L Tociu, DA Case, LC Seefeldt… - Journal of the …, 2019 - ACS Publications
We have shown that the key state in N2 reduction to two NH3 molecules by the enzyme
nitrogenase is E4 (4H), the “Janus” intermediate, which has accumulated four [e–/H+] and is …

Electron Redistribution within the Nitrogenase Active Site FeMo-Cofactor During Reductive Elimination of H2 to Achieve N≡N Triple-Bond Activation

DA Lukoyanov, ZY Yang, DR Dean… - Journal of the …, 2020 - ACS Publications
Nitrogen fixation by nitrogenase begins with the accumulation of four reducing equivalents
at the active-site FeMo-cofactor (FeMo-co), generating a state (denoted E4 (4H)) with two [Fe …