Search for Articles:
Title / Keyword
Author / Affiliation / Email
Journal
Article Type
 
 
Advanced Search
 
Section
Special Issue
Volume
Issue
Number
Page
 
6.7
4.6
Journals
Molecules
Special Issues
Latest Discoveries in Metalloproteins
molecules-logo
Submit to Molecules Review for Molecules Propose a Special Issue

Journal Menu

► Journal Menu

Journal Browser

► Journal Browser
share announcement

Latest Discoveries in Metalloproteins

A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Inorganic Chemistry".

Deadline for manuscript submissions: closed (28 February 2023) | Viewed by 14463

Special Issue Editors

Dr. Ruijie Zhang

E-Mail Website
Guest Editor
Department of Chemistry, Duke University, Durham, NC 27708, USA
Interests: electron transfer; enzyme catalysis; computational chemistry
Dr. Alexander Angerhofer

E-Mail Website
Guest Editor
Department of Chemistry, University of Florida, P.O. Box 117200, Gainesville, FL 32611, USA
Interests: transition-metal-containing enzymes; electron paramagnetic resonance

Special Issue Information

Dear Colleagues,

Metalloproteins are ubiquitous in nature and central to many key biological processes. With advancements in experimental and computational techniques, we are at a point where characterizing enzymatic structure, function, and design has greatly accelerated. To curate the latest discoveries in the fast-growing field of metalloproteins, we invite you to contribute an original research paper or review article in the following areas:

  • Enzymatic catalysis;
  • Inhibitor function and design;
  • Electron transfer;
  • Energy transfer;
  • Protein function and design;
  • Protein–nucleic acid interactions.

Dr. Ruijie Zhang
Dr. Alexander Angerhofer
Guest Editors

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. Molecules is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). 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

  • enzymatic catalysis
  • inhibitor function/design
  • electron transfer
  • energy transfer
  • protein function/design
  • protein–nucleic acid interactions

Published Papers (6 papers)

Download All Papers
Order results
Result details
Show export options expand_more Show export options expand_less
Select all
Export citation of selected articles as:

Research

Jump to: Review

11 pages, 3261 KiB  
Article
Efficient Degradation of Tetracycline Antibiotics by Engineered Myoglobin with High Peroxidase Activity
by Guang-Rong Wu, Li-Juan Sun, Jia-Kun Xu, Shu-Qin Gao, Xiang-Shi Tan and Ying-Wu Lin
Molecules 2022, 27(24), 8660; https://doi.org/10.3390/molecules27248660 - 7 Dec 2022
Cited by 8 | Viewed by 1944
Abstract
Tetracyclines are one class of widely used antibiotics. Meanwhile, due to abuse and improper disposal, they are often detected in wastewater, which causes a series of environmental problems and poses a threat to human health and safety. As an efficient and environmentally friendly [...] Read more.
Tetracyclines are one class of widely used antibiotics. Meanwhile, due to abuse and improper disposal, they are often detected in wastewater, which causes a series of environmental problems and poses a threat to human health and safety. As an efficient and environmentally friendly method, enzymatic catalysis has attracted much attention. In previous studies, we have designed an efficient peroxidase (F43Y/P88W/F138W Mb, termed YWW Mb) based on the protein scaffold of myoglobin (Mb), an O2 carrier, by modifying the heme active center and introducing two Trp residues. In this study, we further applied it to degrade the tetracycline antibiotics. Both UV-Vis and HPLC studies showed that the triple mutant YWW Mb was able to catalyze the degradation of tetracycline, oxytetracycline, doxycycline, and chlortetracycline effectively, with a degradation rate of ~100%, ~98%, ~94%, and ~90%, respectively, within 5 min by using H2O2 as an oxidant. These activities are much higher than those of wild-type Mb and other heme enzymes such as manganese peroxidase. As further analyzed by UPLC-ESI-MS, we identified multiple degradation products and thus proposed possible degradation mechanisms. In addition, the toxicity of the products was analyzed by using in vitro antibacterial experiments of E. coli. Therefore, this study indicates that the engineered heme enzyme has potential applications for environmental remediation by degradation of tetracycline antibiotics. Full article
(This article belongs to the Special Issue Latest Discoveries in Metalloproteins)
►▼ Show Figures

Figure 1

24 pages, 12183 KiB  
Article
Differential Expression and Localization of ADAMTS Proteinases in Proliferative Diabetic Retinopathy
by Ahmed M. Abu El-Asrar, Mohd Imtiaz Nawaz, Eef Allegaert, Mohammad Mairaj Siddiquei, Ajmal Ahmad, Priscilla Gikandi, Gert De Hertogh and Ghislain Opdenakker
Molecules 2022, 27(18), 5977; https://doi.org/10.3390/molecules27185977 - 14 Sep 2022
Cited by 2 | Viewed by 1773
Abstract
We analyzed the expression of ADAMTS proteinases ADAMTS-1, -2, -4, -5 and -13; their activating enzyme MMP-15; and the degradation products of proteoglycan substrates versican and biglycan in an ocular microenvironment of proliferative diabetic retinopathy (PDR) patients. Vitreous samples from PDR and nondiabetic [...] Read more.
We analyzed the expression of ADAMTS proteinases ADAMTS-1, -2, -4, -5 and -13; their activating enzyme MMP-15; and the degradation products of proteoglycan substrates versican and biglycan in an ocular microenvironment of proliferative diabetic retinopathy (PDR) patients. Vitreous samples from PDR and nondiabetic patients, epiretinal fibrovascular membranes from PDR patients, rat retinas, retinal Müller glial cells and human retinal microvascular endothelial cells (HRMECs) were studied. The levels of ADAMTS proteinases and MMP-15 were increased in the vitreous from PDR patients. Both full-length and cleaved activation/degradation fragments of ADAMTS proteinases were identified. The amounts of versican and biglycan cleavage products were increased in vitreous from PDR patients. ADAMTS proteinases and MMP-15 were localized in endothelial cells, monocytes/macrophages and myofibroblasts in PDR membranes, and ADAMTS-4 was expressed in the highest number of stromal cells. The angiogenic activity of PDR membranes correlated significantly with levels of ADAMTS-1 and -4 cellular expression. ADAMTS proteinases and MMP-15 were expressed in rat retinas. ADAMTS-1 and -5 and MMP-15 levels were increased in diabetic rat retinas. HRMECs and Müller cells constitutively expressed ADAMTS proteinases but not MMP-15. The inhibition of NF-κB significantly attenuated the TNF-α-and-VEGF-induced upregulation of ADAMTS-1 and -4 in a culture medium of HRMECs and Müller cells. In conclusion, ADAMTS proteinases, MMP-15 and versican and biglycan cleavage products were increased in the ocular microenvironment of patients with PDR. Full article
(This article belongs to the Special Issue Latest Discoveries in Metalloproteins)
►▼ Show Figures

Figure 1

11 pages, 1787 KiB  
Article
The Influence of Different Bleaching Protocols on Dentinal Enzymatic Activity: An In Vitro Study
by Eric Mayer-Santos, Tatjana Maravic, Allegra Comba, Patricia Moreira Freitas, Giovanna Bueno Marinho, Claudia Mazzitelli, Edoardo Mancuso, Nicola Scotti, Federica Florenzano, Lorenzo Breschi and Annalisa Mazzoni
Molecules 2022, 27(5), 1684; https://doi.org/10.3390/molecules27051684 - 4 Mar 2022
Cited by 3 | Viewed by 2021
Abstract
This study aimed to investigate matrix metalloproteinase (MMP) activity in human dentin using in-situ and gelatin zymography, after at-home and in-office bleaching, related to their clinical exposure times. Dentin specimens (n = 5) were treated with 35% hydrogen peroxide (50 min per [...] Read more.
This study aimed to investigate matrix metalloproteinase (MMP) activity in human dentin using in-situ and gelatin zymography, after at-home and in-office bleaching, related to their clinical exposure times. Dentin specimens (n = 5) were treated with 35% hydrogen peroxide (50 min per session/4 sessions), 10% carbamide peroxide (180 min/21 sessions), or no treatment. All were subjected to in-situ zymography. Dentin slices were, subsequently, obtained, covered with fluorescein-conjugated gelatin, and examined with confocal laser-scanning microscopy. The fluorescence intensity was quantified and statistically analyzed using one-way ANOVA and Bonferroni tests (α = 0.05). Furthermore, gelatin zymography was performed on protein extracts obtained from dentin powder (N = 8 teeth), treated with hydrogen peroxide or carbamide peroxide, with different exposure times (10/50 min for hydrogen peroxide; 252/1260 min for carbamide peroxide). The results of the in-situ zymography showed no statistical differences between the bleached specimens and the control group, with a medium level of gelatinolytic activity expressed in the dentin tubules. The results of gelatin zymography showed an increased expression of pro-MMP-9 in carbamide peroxide groups. The expression of pro-MMP-2 decreased in all the experimental groups. The bleaching treatments performed on the enamel of sound teeth do not influence dentinal enzymatic activity. However, when unprotected dentin tissue is bleached, matrix metalloproteinases are more expressed, particularly when carbamide peroxide is used, proportional to the exposure time. Full article
(This article belongs to the Special Issue Latest Discoveries in Metalloproteins)
►▼ Show Figures

Figure 1

Review

Jump to: Research

13 pages, 4109 KiB  
Review
Laccase Engineering: Redox Potential Is Not the Only Activity-Determining Feature in the Metalloproteins
by Misha Ali, Priyanka Bhardwaj, Hassan Mubarak Ishqi, Mohammad Shahid and Asimul Islam
Molecules 2023, 28(17), 6209; https://doi.org/10.3390/molecules28176209 - 23 Aug 2023
Cited by 3 | Viewed by 1448
Abstract
Laccase, one of the metalloproteins, belongs to the multicopper oxidase family. It oxidizes a wide range of substrates and generates water as a sole by-product. The engineering of laccase is important to broaden their industrial and environmental applications. The general assumption is that [...] Read more.
Laccase, one of the metalloproteins, belongs to the multicopper oxidase family. It oxidizes a wide range of substrates and generates water as a sole by-product. The engineering of laccase is important to broaden their industrial and environmental applications. The general assumption is that the low redox potential of laccases is the principal obstacle, as evidenced by their low activity towards certain substrates. Therefore, the primary goal of engineering laccases is to improve their oxidation capability, thereby increasing their redox potential. Even though some of the determinants of laccase are known, it is still not entirely clear how to enhance its redox potential. However, the laccase active site has additional characteristics that regulate the enzymes’ activity and specificity. These include the electrostatic and hydrophobic environment of the substrate binding pocket, the steric effect at the substrate binding site, and the orientation of the binding substrate with respect to the T1 site of the laccase. In this review, these features of the substrate binding site will be discussed to highlight their importance as a target for future laccase engineering. Full article
(This article belongs to the Special Issue Latest Discoveries in Metalloproteins)
►▼ Show Figures

Figure 1

28 pages, 960 KiB  
Review
The Role of MMP-9 and MMP-9 Inhibition in Different Types of Thyroid Carcinoma
by Zhenshengnan Li, Jia Wei, Bowen Chen, Yaoqi Wang, Shuai Yang, Kehui Wu and Xianying Meng
Molecules 2023, 28(9), 3705; https://doi.org/10.3390/molecules28093705 - 25 Apr 2023
Cited by 6 | Viewed by 2102
Abstract
Matrix metalloproteinase-9 (MMP-9), one of the most investigated and studied biomarkers of the MMPs family, is a zinc-dependent proteolytic metalloenzyme whose primary function is degrading the extracellular matrix (ECM). It has been proved that MMP-9 expression elevates in multiple pathological conditions, including thyroid [...] Read more.
Matrix metalloproteinase-9 (MMP-9), one of the most investigated and studied biomarkers of the MMPs family, is a zinc-dependent proteolytic metalloenzyme whose primary function is degrading the extracellular matrix (ECM). It has been proved that MMP-9 expression elevates in multiple pathological conditions, including thyroid carcinoma. MMP-9 has a detectable higher level in malignant or metastatic thyroid tumor tissues than in normal or benign tissues and acts as an additional marker to distinguish different tumor stages because of its close correlations with clinical features, such as lymph node metastasis, TNM stage, tumor size and so on. Natural and non-natural MMP-9 inhibitors suppress its expression, block the progression of diseases, and play a role in therapy consequently. MMP-9 inhibitory molecules also assist in treating thyroid tumors by suppressing the proliferation, invasion, migration, metastasis, viability, adhesion, motility, epithelial-mesenchymal transition (EMT), and other risk factors of different thyroid cancer cells. In a word, discovering and designing MMP-9 inhibitors provide great therapeutic effects and promising clinical values in various types of thyroid carcinoma. Full article
(This article belongs to the Special Issue Latest Discoveries in Metalloproteins)
►▼ Show Figures

Figure 1

14 pages, 1693 KiB  
Review
Machine Learning Approaches for Metalloproteins
by Yue Yu, Ruobing Wang and Ruijie D. Teo
Molecules 2022, 27(4), 1277; https://doi.org/10.3390/molecules27041277 - 14 Feb 2022
Cited by 5 | Viewed by 4325
Abstract
Metalloproteins are a family of proteins characterized by metal ion binding, whereby the presence of these ions confers key catalytic and ligand-binding properties. Due to their ubiquity among biological systems, researchers have made immense efforts to predict the structural and functional roles of [...] Read more.
Metalloproteins are a family of proteins characterized by metal ion binding, whereby the presence of these ions confers key catalytic and ligand-binding properties. Due to their ubiquity among biological systems, researchers have made immense efforts to predict the structural and functional roles of metalloproteins. Ultimately, having a comprehensive understanding of metalloproteins will lead to tangible applications, such as designing potent inhibitors in drug discovery. Recently, there has been an acceleration in the number of studies applying machine learning to predict metalloprotein properties, primarily driven by the advent of more sophisticated machine learning algorithms. This review covers how machine learning tools have consolidated and expanded our comprehension of various aspects of metalloproteins (structure, function, stability, ligand-binding interactions, and inhibitors). Future avenues of exploration are also discussed. Full article
(This article belongs to the Special Issue Latest Discoveries in Metalloproteins)
►▼ Show Figures

Graphical abstract

Show export options expand_more Show export options expand_less
Select all
Export citation of selected articles as:
 
Displaying articles 1-6
Back to TopTop