Designing artificial metalloenzymes by tuning of the environment beyond the primary coordination sphere
Metalloenzymes catalyze a variety of reactions using a limited number of natural amino
acids and metallocofactors. Therefore, the environment beyond the primary coordination …
acids and metallocofactors. Therefore, the environment beyond the primary coordination …
Oxygen activation and radical transformations in heme proteins and metalloporphyrins
As a result of the adaptation of life to an aerobic environment, nature has evolved a panoply
of metalloproteins for oxidative metabolism and protection against reactive oxygen species …
of metalloproteins for oxidative metabolism and protection against reactive oxygen species …
Second sphere effects on oxygen reduction and peroxide activation by mononuclear iron porphyrins and related systems
Activation and reduction of O2 and H2O2 by synthetic and biosynthetic iron porphyrin
models have proved to be a versatile platform for evaluating second-sphere effects deemed …
models have proved to be a versatile platform for evaluating second-sphere effects deemed …
Synthetic Fe/Cu complexes: toward understanding heme-copper oxidase structure and function
Heme-copper oxidases (HCOs) are terminal enzymes on the mitochondrial or bacterial
respiratory electron transport chain, which utilize a unique heterobinuclear active site to …
respiratory electron transport chain, which utilize a unique heterobinuclear active site to …
Activation of dioxygen by copper metalloproteins and insights from model complexes
Nature uses dioxygen as a key oxidant in the transformation of biomolecules. Among the
enzymes that are utilized for these reactions are copper-containing metalloenzymes, which …
enzymes that are utilized for these reactions are copper-containing metalloenzymes, which …
In situ structural observation of a substrate-and peroxide-bound high-spin ferric-hydroperoxo intermediate in the P450 enzyme CYP121
The P450 enzyme CYP121 from Mycobacterium tuberculosis catalyzes a carbon–carbon (C–
C) bond coupling cyclization of the dityrosine substrate containing a diketopiperazine ring …
C) bond coupling cyclization of the dityrosine substrate containing a diketopiperazine ring …
Molecular understanding of heteronuclear active sites in heme–copper oxidases, nitric oxide reductases, and sulfite reductases through biomimetic modelling
CJ Reed, QN Lam, EN Mirts, Y Lu - Chemical Society Reviews, 2021 - pubs.rsc.org
Heme–copper oxidases (HCO), nitric oxide reductases (NOR), and sulfite reductases (SiR)
catalyze the multi-electron and multi-proton reductions of O2, NO, and SO32−, respectively …
catalyze the multi-electron and multi-proton reductions of O2, NO, and SO32−, respectively …
Single metal atom catalysts and ORR: H-bonding, solvation, and the elusive hydroperoxyl intermediate
F Armillotta, D Bidoggia, S Baronio, P Biasin… - ACS …, 2022 - ACS Publications
The widely investigated oxygen reduction reaction (ORR) is well-known to proceed via two
competing routes, involving two or four electrons, and yielding different reaction products …
competing routes, involving two or four electrons, and yielding different reaction products …
Design of artificial metalloproteins/metalloenzymes by tuning noncovalent interactions
S Hirota, YW Lin - JBIC Journal of Biological Inorganic Chemistry, 2018 - Springer
Noncovalent weak interactions [hydrophobic interaction and hydrogen (H)-bond] play crucial
roles in controlling the functions of biomolecules, and thus have been used to design …
roles in controlling the functions of biomolecules, and thus have been used to design …
Molecular rationale for partitioning between C–H and C–F bond activation in heme-dependent tyrosine hydroxylase
The heme-dependent l-tyrosine hydroxylases (TyrHs) in natural product biosynthesis
constitute a new enzyme family in contrast to the nonheme iron enzymes for DOPA …
constitute a new enzyme family in contrast to the nonheme iron enzymes for DOPA …