The spectroscopy of nitrogenases
Nitrogenases are responsible for biological nitrogen fixation, a crucial step in the
biogeochemical nitrogen cycle. These enzymes utilize a two-component protein system and …
biogeochemical nitrogen cycle. These enzymes utilize a two-component protein system and …
High-Resolution ENDOR Spectroscopy Combined with Quantum Chemical Calculations Reveals the Structure of Nitrogenase Janus Intermediate E4(4H)
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 …
nitrogenase is E4 (4H), the “Janus” intermediate, which has accumulated four [e–/H+] and is …
Understanding the Electronic Structure Basis for N2 Binding to FeMoco: A Systematic Quantum Mechanics/Molecular Mechanics Investigation
Y Pang, R Bjornsson - Inorganic Chemistry, 2023 - ACS Publications
The FeMo cofactor (FeMoco) of Mo nitrogenase is responsible for reducing dinitrogen to
ammonia, but it requires the addition of 3–4 e–/H+ pairs before N2 even binds. A binding …
ammonia, but it requires the addition of 3–4 e–/H+ pairs before N2 even binds. A binding …
N 2 binding to the E 0–E 4 states of nitrogenase
Nitrogenase is the only enzyme that can convert N2 into NH3. The reaction requires the
addition of eight electrons and protons to the enzyme and the mechanism is normally …
addition of eight electrons and protons to the enzyme and the mechanism is normally …
How feasible is the reversible S-dissociation mechanism for the activation of FeMo-co, the catalytic site of nitrogenase?
I Dance - Dalton Transactions, 2019 - pubs.rsc.org
The active site of the enzyme nitrogenase (N2→ NH3) is a Fe7MoS9C cluster that contains
three doubly-bridging μ-S atoms around a central belt. A vanadium nitrogenase variant has …
three doubly-bridging μ-S atoms around a central belt. A vanadium nitrogenase variant has …
H 2 formation from the E 2–E 4 states of nitrogenase
Nitrogenase is the only enzyme that can cleave the strong triple bond in N2, making nitrogen
available for biological lifeforms. The active site is a MoFe7S9C cluster (the FeMo cluster) …
available for biological lifeforms. The active site is a MoFe7S9C cluster (the FeMo cluster) …
Mixed-valent diiron μ-carbyne, μ-hydride complexes: Implications for nitrogenase
CH Arnett, I Bogacz, R Chatterjee, J Yano… - Journal of the …, 2020 - ACS Publications
Binding of N2 by the FeMo-cofactor of nitrogenase is believed to occur after transfer of 4 e–
and 4 H+ equivalents to the active site. Although pulse EPR studies indicate the presence of …
and 4 H+ equivalents to the active site. Although pulse EPR studies indicate the presence of …
Mechanism of Nitrogen Reduction to Ammonia in a Diiron Model of Nitrogenase
M Barchenko, PJ O'Malley, SP de Visser - Inorganic Chemistry, 2023 - ACS Publications
Nitrogenase is a fascinating enzyme in biology that reduces dinitrogen from air to ammonia
through stepwise reduction and protonation. Despite it being studied in detail by …
through stepwise reduction and protonation. Despite it being studied in detail by …
Putative reaction mechanism of nitrogenase with a half-dissociated S2B ligand
We have studied whether dissociation of the S2B sulfide ligand from one of its two
coordinating Fe ions may affect the later parts of the reaction mechanism of nitrogenase …
coordinating Fe ions may affect the later parts of the reaction mechanism of nitrogenase …
Scalar Relativistic All-Electron and Pseudopotential Ab Initio Study of a Minimal Nitrogenase [Fe(SH)4H]− Model Employing Coupled-Cluster and Auxiliary-Field …
VP Vysotskiy, C Filippi, U Ryde - The Journal of Physical …, 2024 - ACS Publications
Nitrogenase is the only enzyme that can cleave the triple bond in N2, making nitrogen
available to organisms. The detailed mechanism of this enzyme is currently not known, and …
available to organisms. The detailed mechanism of this enzyme is currently not known, and …