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Zayed, A., M. K. Mansour, M. S. Sedeek, M. H. Habib, R. Ulber, and M. A. Farag, "Rediscovering bacterial exopolysaccharides of terrestrial and marine origins:novel insights on their distribution, biosynthesis, biotechnological production, and future perspectives", Critical Reviews in Biotechnology, 2021.
Salama, S., T. Dishisha, M. H. Habib, A. Z. Abdelazem, W. Bakeer, M. Abdel-Latif, and Y. Gaber, "Enantioselective sulfoxidation using Streptomyces glaucescens GLA.0", RSC Advances, vol. 10, issue 54: The Royal Society of Chemistry, pp. 32335-32344, 2020. Abstract
Zitare, U. A., M. H. Habib, H. Rozeboom, M. L. Mascotti, S. Todorovic, and M. W. Fraaije, "Mutational and structural analysis of an ancestral fungal dye-decolorizing peroxidase.", The FEBS journal, 2020. Abstract

Dye-decolorizing peroxidases (DyPs) constitute a superfamily of heme-containing peroxidases that are related neither to animal nor to plant peroxidase families. These are divided into four classes (types A, B, C, and D) based on sequence features. The active site of DyPs contains two highly conserved distal ligands, an aspartate and an arginine, the roles of which are still controversial. These ligands have mainly been studied in class A-C bacterial DyPs, largely because no effective recombinant expression systems have been developed for the fungal (D-type) DyPs. In this work, we employ ancestral sequence reconstruction (ASR) to resurrect a D-type DyP ancestor, AncDyPD-b1. Expression of AncDyPD-b1 in Escherichia coli results in large amounts of a heme-containing soluble protein and allows for the first mutagenesis study on the two distal ligands of a fungal DyP. UV-Vis and resonance Raman (RR) spectroscopic analyses, in combination with steady-state kinetics and the crystal structure, reveal fine pH-dependent details about the heme active site structure and show that both the aspartate (D222) and the arginine (R390) are crucial for hydrogen peroxide reduction. Moreover, the data indicate that these two residues play important but mechanistically different roles on the intraprotein long-range electron transfer process. DATABASE: Structural data are available in the PDB database under the accession number 7ANV.

Habib, M. H., M. Trajkovic, and M. W. Fraaije, "Oxidative Methods: Synthesis of Syringaresinol from 2,6-Dimethoxy-4-Allylphenol Using an Oxidase/Peroxidase Enzyme System", Applied Biocatalysis: The Chemist's Enzyme Toolbox: Wiley, pp. 301-307, 2020. Abstract
Habib, M. H., H. J. Rozeboom, and M. W. Fraaije, "Characterization of a New DyP-Peroxidase from the Alkaliphilic Cellulomonad, Cellulomonas bogoriensis", Molecules, vol. 24, issue 7: MDPI, pp. 1208, 2019. Abstract
Habib, M., M. Trajkovic, and M. W. Fraaije, "The biocatalytic synthesis of syringaresinol from 2, 6-dimethoxy-4-allylphenol in one-pot using a tailored oxidase/peroxidase system", ACS Catalysis, vol. 8, issue 6: American Chemical Society, pp. 5549-5552, 2018. Abstract
Habib, M. H. M., P. J. Deuss, N. Lončar, M. Trajkovic, and M. W. Fraaije, "A Biocatalytic One‐Pot Approach for the Preparation of Lignin Oligomers Using an Oxidase/Peroxidase Cascade Enzyme System", Advanced Synthesis & Catalysis, vol. 359, issue 19, pp. 3354-3361, 2017. Abstract
de Gonzalo, G., D. I. Colpa, M. H. M. Habib, and M. W. Fraaije, "Bacterial enzymes involved in lignin degradation", Journal of Biotechnology, vol. 236: Elsevier, pp. 110-119, 2016. Abstract