@article{ba7601bd085943299c289b07a848a0e0,
title = "Histidine orientation in artificial peroxidase regioisomers as determined by paramagnetic NMR shifts",
abstract = "Fe-Mimochrome VI*a is a synthetic peroxidase and peroxygenase, featuring two different peptides that are covalently-linked to deuteroheme. To perform a systematic structure/function correlation, we purposely shortened the distance between the distal peptide and the heme, allowing for the separation and characterization of two regioisomers. They differ in both His axial-ligand orientation, as determined by paramagnetic NMR shifts, and activity. These findings highlight that synthetic metalloenzymes may provide an efficient tool for disentangling the role of axial ligand orientation over peroxidase activity.",
author = "Ornella Maglio and Marco Chino and Claudia Vicari and Vincenzo Pavone and Louro, {Ricardo O.} and Angela Lombardi",
note = "Funding Information: The authors thank to Corinne Cerrone for synthesizing the Fe-Lys9DabMC6*a, and Monica Grasso for technical assistance. This work is part of collaboration under COST action CM1003 (Biological Oxidation Reactions: Mechanisms and Design of New Catalysts). Financial support was provided by Campania Region (Programma Operativo FESR Campania 2014 – 2020, Asse 1 – CUP B63D18000350007), and by European EC Horizon2020 TIMB3 (Project 810856). This work was also funded by national funds through FCT – Funda{\c c}{\~a}o para a Ci{\^e}ncia e a Tecnologia, I. P., Project MOSTMICRO-ITQB with refs UIDB/04612/2020 and UIDP/04612/2020, and project PTDC/BIA-BQM/30176/2017. The NMR data were acquired at CERMAX, ITQB-NOVA, Oeiras, Portugal, with equipment funded by FCT, project AAC01/ SAICT/2016. Publisher Copyright: {\textcopyright} The Royal Society of Chemistry 2021.",
year = "2021",
month = jan,
day = "25",
doi = "10.1039/d0cc06676a",
language = "English",
volume = "57",
pages = "990--993",
journal = "Chemical Communications",
issn = "1359-7345",
publisher = "RSC - Royal Society of Chemistry",
number = "8",
}