Designing artificial metalloenzymes by tuning of the environment beyond the primary coordination sphere

C Van Stappen, Y Deng, Y Liu, H Heidari… - Chemical …, 2022 - ACS Publications
Metalloenzymes catalyze a variety of reactions using a limited number of natural amino
acids and metallocofactors. Therefore, the environment beyond the primary coordination …

Second sphere effects on oxygen reduction and peroxide activation by mononuclear iron porphyrins and related systems

S Bhunia, A Ghatak, A Dey - Chemical Reviews, 2022 - ACS Publications
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 …

Synthetic Fe/Cu complexes: toward understanding heme-copper oxidase structure and function

SM Adam, GB Wijeratne, PJ Rogler, DE Diaz… - Chemical …, 2018 - ACS Publications
Heme-copper oxidases (HCOs) are terminal enzymes on the mitochondrial or bacterial
respiratory electron transport chain, which utilize a unique heterobinuclear active site to …

Understanding and modulating metalloenzymes with unnatural amino acids, non-native metal ions, and non-native metallocofactors

EN Mirts, A Bhagi-Damodaran, Y Lu - Accounts of chemical …, 2019 - ACS Publications
Conspectus Metalloproteins set the gold standard for performing important functions,
including catalyzing demanding reactions under mild conditions. Designing artificial …

Design and engineering of artificial oxygen-activating metalloenzymes

F Nastri, M Chino, O Maglio… - Chemical Society …, 2016 - pubs.rsc.org
Many efforts are being made in the design and engineering of metalloenzymes with catalytic
properties fulfilling the needs of practical applications. Progress in this field has recently …

Why copper is preferred over iron for oxygen activation and reduction in haem-copper oxidases

A Bhagi-Damodaran, MA Michael, Q Zhu, J Reed… - Nature …, 2017 - nature.com
Haem–copper oxidase (HCO) catalyses the natural reduction of oxygen to water using a
haem-copper centre. Despite decades of research on HCOs, the role of non-haem metal …

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 …

[HTML][HTML] Transient β-hairpin formation in α-synuclein monomer revealed by coarse-grained molecular dynamics simulation

H Yu, W Han, W Ma, K Schulten - The Journal of chemical physics, 2015 - pubs.aip.org
Parkinson's disease, originating from the intrinsically disordered peptide α-synuclein, is a
common neurodegenerative disorder that affects more than 5% of the population above age …

Engineering metalloprotein functions in designed and native scaffolds

F Nastri, D D'Alonzo, L Leone, G Zambrano… - Trends in biochemical …, 2019 - cell.com
Metalloproteins are crucial for life. The mutual relationship between metal ions and proteins
makes metalloproteins able to accomplish key processes in biological systems, often very …

Systematic Tuning of Heme Redox Potentials and Its Effects on O2 Reduction Rates in a Designed Oxidase in Myoglobin

A Bhagi-Damodaran, ID Petrik… - Journal of the …, 2014 - ACS Publications
Cytochrome c Oxidase (C c O) is known to catalyze the reduction of O2 to H2O efficiently
with a much lower overpotential than most other O2 reduction catalysts. However, methods …