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The biologically relevant coordination chemistry of iron and nitric oxide: electronic structure and reactivity
Nitric oxide (NO) is an important signaling molecule that is involved in a wide range of
physiological and pathological events in biology. Metal coordination chemistry, especially …
physiological and pathological events in biology. Metal coordination chemistry, especially …
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 …
Advances in the Chemistry of Oxaziridines
Oxaziridines constitute a subset of a class of versatile oxidants whose characteristic feature
is the presence of two electronegative heteroatoms within a strained three-membered ring …
is the presence of two electronegative heteroatoms within a strained three-membered ring …
Comparative electronic structures of nitrogenase FeMoco and FeVco
An investigation of the active site cofactors of the molybdenum and vanadium nitrogenases
(FeMoco and FeVco) was performed using high-resolution X-ray spectroscopy. Synthetic …
(FeMoco and FeVco) was performed using high-resolution X-ray spectroscopy. Synthetic …
Non‐Heme Imine‐Based Iron Complexes as Catalysts for Oxidative Processes
Non‐heme iron complexes are emerging as powerful and versatile catalysts in several
oxidative transformations. The most investigated iron complex structures are based on …
oxidative transformations. The most investigated iron complex structures are based on …
Spectroscopic Description of the E1 State of Mo Nitrogenase Based on Mo and Fe X-ray Absorption and Mössbauer Studies
Mo nitrogenase (N2ase) utilizes a two-component protein system, the catalytic MoFe and its
electron-transfer partner FeP, to reduce atmospheric dinitrogen (N2) to ammonia (NH3). The …
electron-transfer partner FeP, to reduce atmospheric dinitrogen (N2) to ammonia (NH3). The …
Addition of Dioxygen to an N4S(thiolate) Iron(II) Cysteine Dioxygenase Model Gives a Structurally Characterized Sulfinato–Iron(II) Complex
AC McQuilken, Y Jiang, MA Siegler… - Journal of the …, 2012 - ACS Publications
The non-heme iron enzyme cysteine dioxygenase (CDO) catalyzes the S-oxygenation of
cysteine by O2 to give cysteine sulfinic acid. The synthesis of a new structural and functional …
cysteine by O2 to give cysteine sulfinic acid. The synthesis of a new structural and functional …
Understanding how the thiolate sulfur contributes to the function of the non-heme iron enzyme superoxide reductase
JA Kovacs, LM Brines - Accounts of chemical research, 2007 - ACS Publications
Toxic superoxide radicals, generated via adventitious reduction of dioxygen, have been
implicated in a number of disease states. The cysteinate-ligated non-heme iron enzyme …
implicated in a number of disease states. The cysteinate-ligated non-heme iron enzyme …
Correlation Between Structural, Spectroscopic, and Reactivity Properties Within a Series of Structurally Analogous Metastable Manganese (III)–Alkylperoxo …
MK Coggins, V Martin-Diaconescu… - Journal of the …, 2013 - ACS Publications
Manganese–peroxos are proposed as key intermediates in a number of important
biochemical and synthetic transformations. Our understanding of the structural …
biochemical and synthetic transformations. Our understanding of the structural …
Role of second-sphere arginine residues in metal binding and metallocentre assembly in nitrile hydratases
Two conserved second-sphere βArg (R) residues in nitrile hydratases (NHase), that form
hydrogen bonds with the catalytically essential sulfenic and sulfinic acid ligands, were …
hydrogen bonds with the catalytically essential sulfenic and sulfinic acid ligands, were …