Meanings of dioxygen in English

Copper active sites play a major role in enzymatic activation of dioxygen.

An indole-dioxygen adduct has been built which fits the electron density convincingly.

This network transports protons in the four-electron reduction of dioxygen.

The hydrogen bonding in their corresponding dioxygen adducts is directly measured by pulse EPR spectroscopy.

The plausible location for the binding of dioxygen is between this pocket and the catalytic iron.

These enzymes utilize a mononuclear non-heme iron center to catalyze the addition of dioxygen to their respective substrates.

The reaction of ferrous bleomycin with dioxygen is reexamined to clarify whether radical species derived from molecular oxygen are generated.

These hybrid molecular materials behave as molecular electroanodes that catalyse water oxidation to dioxygen at pH 7 with high current densities.

Given this structure, it is likely that dioxygen is directly involved in the electron transfer and hydrogen abstraction steps of the PHM reaction.

Distal hydrogen bonding in natural dioxygen binding proteins is crucial for the discrimination between different potential ligands such as O(2) or CO.

The single turnover reaction initiated by adding dioxygen to a preformed reduced P450-CAM.Pdx complex with excess camphor also led to phases with similar rates.

Nitric oxide (NO) is commonly used as an analogue for dioxygen in structural and spectroscopic studies of oxygen binding and oxygen activation.

In a complex with substrate and dioxygen, the dioxygen molecule is lined up for an attack on the double bond of the aromatic substrate.

Further, mutation at the Cys ligand gives a vacant type I copper center and traps the reaction intermediate during the four-electron reduction of dioxygen.

In the present study, we probe the chemical requirements for proper distal hydrogen bonding in a series of synthetic model compounds for dioxygen-binding heme proteins.

The flavin reductase system catalyzes the interconversion in both directions with dioxygen as the critical factor deciding whether activation or inactivation of ribonucleotide reductase occurs.