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Molecular Enzymology and Biotechnology for Extreme Environments
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Molecular Enzymology and Biotechnology for Extreme Environments

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Biochemistry".

Deadline for manuscript submissions: closed (30 November 2024) | Viewed by 2819

Special Issue Editor

Dr. Roberta Iacono

E-Mail Website
Guest Editor
Department of Biology, University of Naples Federico II, Complesso Universitario di Monte S. Angelo, Via Cinthia 21, 80126 Naples, Italy
Interests: thermophilic enzymes; carbohydrate active enzymes; green chemistry; extreme environments; enrichment; metagenomic analysis; bioconversions

Special Issue Information

Dear Colleagues,

The increasing demand for environmentally friendly technologies is driving a transition from a linear to a circular bioeconomy. Within this transition, the discovery and use of robust biocatalysts are crucial in obtaining specific bioproduct substitutes. However, most modern industrial processes are carried out in severe conditions; thus, the intrinsic properties of enzymes from extremophiles offer some advantages from an industrial perspective. In recent years, high-throughput sequencing in combination with advanced bioinformatics algorithms has allowed us to enhance and expand our insights into extremophilic microbial taxa, to decipher their functional capacities and activities and reconstruct their roles. However, metagenomics approaches give little information on the expression and function of genes. Only detailed enzymatic characterizations can confirm the inferred activity and evaluate potential applications.

From thriving in extreme environments to unlocking novel biotechnological applications, this Special Issue explores the profound impact of extremozymes in industrial processes. This Special Issue welcomes review, opinion, and research articles that focus on, but are not limited to, the above topics.

Dr. Roberta Iacono
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • extremozymes
  • extreme environments
  • biotechnological applications
  • circular bioeconomy
  • sustainability
  • green economy
  • extremophiles

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Published Papers (2 papers)

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Research

16 pages, 12939 KiB  
Article
A High-Resolution Crystallographic Study of Cytochrome c6: Structural Basis for Electron Transfer in Cyanobacterial Photosynthesis
by Botao Zhang, Yuancong Xu, Shuwen Liu, Sixu Chen, Wencong Zhao, Zhaoyang Li, Junshuai Wang, Weijian Zhao, Heng Zhang, Yuhui Dong, Yong Gong, Wang Sheng and Peng Cao
Int. J. Mol. Sci. 2025, 26(2), 824; https://doi.org/10.3390/ijms26020824 - 19 Jan 2025
Viewed by 1500
Abstract
Cyanobacterial cytochrome c6 (Cyt c6) is crucial for electron transfer between the cytochrome b6f complex and photosystem I (PSI), playing a key role in photosynthesis and enhancing adaptation to extreme environments. This study investigates the high-resolution crystal structures of Cyt c6 from Synechococcus [...] Read more.
Cyanobacterial cytochrome c6 (Cyt c6) is crucial for electron transfer between the cytochrome b6f complex and photosystem I (PSI), playing a key role in photosynthesis and enhancing adaptation to extreme environments. This study investigates the high-resolution crystal structures of Cyt c6 from Synechococcus elongatus PCC 7942 and Synechocystis PCC 6803, focusing on its dimerization mechanisms and functional implications for photosynthesis. Cyt c6 was expressed in Escherichia coli using a dual-plasmid co-expression system and characterized in both oxidized and reduced states. X-ray crystallography revealed three distinct crystal forms, with asymmetric units containing 2, 4, or 12 molecules, all of which consist of repeating dimeric structures. Structural comparisons across species indicated that dimerization predominantly occurs through hydrophobic interactions within a conserved motif around the heme crevice, despite notable variations in dimer positioning. We propose that the dimerization of Cyt c6 enhances structural stability, optimizes electron transfer kinetics, and protects the protein from oxidative damage. Furthermore, we used AlphaFold3 to predict the structure of the PSI-Cyt c6 complex, revealing specific interactions that may facilitate efficient electron transfer. These findings provide new insights into the functional role of Cyt c6 dimerization and its contribution to improving cyanobacterial photosynthetic electron transport. Full article
(This article belongs to the Special Issue Molecular Enzymology and Biotechnology for Extreme Environments)
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12 pages, 1216 KiB  
Article
Precise and Accurate DNA-3′/5-Ends Polishing with Thermus thermophilus Phage vb_Tt72 DNA Polymerase
by Sebastian Dorawa and Tadeusz Kaczorowski
Int. J. Mol. Sci. 2024, 25(24), 13544; https://doi.org/10.3390/ijms252413544 - 18 Dec 2024
Viewed by 866
Abstract
Tt72 DNA polymerase is a newly characterized PolA-type thermostable enzyme derived from the Thermus thermophilus phage vB_Tt72. The enzyme demonstrates strong 3′→5′ exonucleolytic proofreading activity, even in the presence of 1 mM dNTPs. In this study, we examined how the exonucleolytic activity of Tt72 [...] Read more.
Tt72 DNA polymerase is a newly characterized PolA-type thermostable enzyme derived from the Thermus thermophilus phage vB_Tt72. The enzyme demonstrates strong 3′→5′ exonucleolytic proofreading activity, even in the presence of 1 mM dNTPs. In this study, we examined how the exonucleolytic activity of Tt72 DNA polymerase affects the fidelity of DNA synthesis. Using a plasmid-based lacZα gene complementation assay, we determined that the enzyme’s mutation frequency was 2.06 × 10−3, corresponding to an error rate of 1.41 × 10−5. For the exonuclease-deficient variant, the mutation frequency increased to 6.23 × 10−3, with an associated error rate of 4.29 × 10−5. The enzyme retained 3′→5′ exonucleolytic activity at temperatures up to 70 °C but lost it after 10 min of incubation at temperatures above 75 °C. Additionally, we demonstrated that Tt72 DNA polymerase efficiently processes 3′/5′-overhangs and removes a single-nucleotide 3′-dA overhang from PCR products at 55 °C. These characteristics make Tt72 DNA polymerase well suited for specialized molecular cloning applications. Full article
(This article belongs to the Special Issue Molecular Enzymology and Biotechnology for Extreme Environments)
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