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
Metalloenzyme Biogenesis and Biocatalysis
molecules-logo
Submit to Molecules Review for Molecules Propose a Special Issue

Journal Menu

► Journal Menu

Journal Browser

► Journal Browser
share announcement

Metalloenzyme Biogenesis and Biocatalysis

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

Deadline for manuscript submissions: closed (1 May 2022) | Viewed by 10488

Special Issue Editors

Dr. Smilja Todorovic

E-Mail Website
Guest Editor
Instituto de Tecnologia Química e Biológica António Xavier (ITQB-NOVA), Universidade NOVA de Lisboa, av. da República, 2780-157 Oeiras, Portugal
Interests: resonance Raman and SERR spectroscopy; bioelectrocatalysis; metalloproteins; heterogeneous electron transfer; biosensing
Dr. Ricardo O. Louro

E-Mail Website
Guest Editor
Instituto de Tecnologia Química e Biológica António Xavier (ITQB-NOVA), Universidade NOVA de Lisboa, av. da República, 2780-157 Oeiras, Portugal
Interests: NMR spectroscopy; multihemic cytochromes; metal-respiring organisms; microbial fuel cells; metalloproteins
Prof. Dr. Miguel Teixeira

E-Mail Website
Guest Editor
Instituto de Tecnologia Química e Biológica António Xavier (ITQB-NOVA), Universidade NOVA de Lisboa, av. da República, 2780-157 Oeiras, Portugal
Interests: EPR spectroscopy; metalloproteins; ROS detoxification; haem-copper oxygen reductases; di-iron proteins

Special Issue Information

Dear Colleagues,

Metalloproteins and metalloenzymes make up more than 40% of the proteome of living organisms. Their importance is well appreciated, even by the general public, given the widely known example of the red color of blood due to hemoglobin. Indeed, the activity of metalloenzymes has an outsized impact on numerous contemporary societal challenges. They allow us to, e.g., live using oxygen, capture CO2, generate ammonia from the atmospheric nitrogen, degrade toxic exogenous molecules, and produce hydrogen from sustainable sources. The process of their biogenesis involves the uptake, homeostatic control, and delivery of metals to the correct apo-protein at the precise timing to generate the active holoprotein. The controlled assembly of metalloenzymes and further exploration of their catalytic activity is conveniently monitored by spectroscopic methods.

This Special Issue explores the fundamentals and applications of exciting metabolic processes that involve metalloproteins and metalloenzymes, and the tools that allow for their in-detail investigations.

Dr. Smilja Todorovic
Dr. Ricardo O. Louro
Prof. Dr. Miguel Teixeira
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

  • Fe-S containing proteins
  • hemeproteins
  • paramagnetic NMR spectroscopy
  • EPR spectroscopy of metalloproteins
  • resonance Raman and IR biospectroscopy
  • enzymatic biocatalysis

Published Papers (4 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

13 pages, 2234 KiB  
Article
Protein Interactions in Rhodopseudomonas palustris TIE-1 Reveal the Molecular Basis for Resilient Photoferrotrophic Iron Oxidation
by Inês B. Trindade, Maria O. Firmino, Sander J. Noordam, Alexandra S. Alves, Bruno M. Fonseca, Mario Piccioli and Ricardo O. Louro
Molecules 2023, 28(12), 4733; https://0-doi-org.brum.beds.ac.uk/10.3390/molecules28124733 - 13 Jun 2023
Cited by 2 | Viewed by 1061
Abstract
Rhodopseudomonas palustris is an alphaproteobacterium with impressive metabolic versatility, capable of oxidizing ferrous iron to fix carbon dioxide using light energy. Photoferrotrophic iron oxidation is one of the most ancient metabolisms, sustained by the pio operon coding for three proteins: PioB and PioA, [...] Read more.
Rhodopseudomonas palustris is an alphaproteobacterium with impressive metabolic versatility, capable of oxidizing ferrous iron to fix carbon dioxide using light energy. Photoferrotrophic iron oxidation is one of the most ancient metabolisms, sustained by the pio operon coding for three proteins: PioB and PioA, which form an outer-membrane porin–cytochrome complex that oxidizes iron outside of the cell and transfers the electrons to the periplasmic high potential iron–sulfur protein (HIPIP) PioC, which delivers them to the light-harvesting reaction center (LH-RC). Previous studies have shown that PioA deletion is the most detrimental for iron oxidation, while, the deletion of PioC resulted in only a partial loss. The expression of another periplasmic HiPIP, designated Rpal_4085, is strongly upregulated in photoferrotrophic conditions, making it a strong candidate for a PioC substitute. However, it is unable to reduce the LH-RC. In this work we used NMR spectroscopy to map the interactions between PioC, PioA, and the LH-RC, identifying the key amino acid residues involved. We also observed that PioA directly reduces the LH-RC, and this is the most likely substitute upon PioC deletion. By contrast, Rpal_4085 demontrated significant electronic and structural differences from PioC. These differences likely explain its inability to reduce the LH-RC and highlight its distinct functional role. Overall, this work reveals the functional resilience of the pio operon pathway and further highlights the use of paramagnetic NMR for understanding key biological processes. Full article
(This article belongs to the Special Issue Metalloenzyme Biogenesis and Biocatalysis)
►▼ Show Figures

Figure 1

15 pages, 2473 KiB  
Article
Disentangling Unusual Catalytic Properties and the Role of the [4Fe-4S] Cluster of Three Endonuclease III from the Extremophile D. radiodurans
by Filipe Rollo, Patricia T. Borges, Célia M. Silveira, Margarida T. G. Rosa, Smilja Todorovic and Elin Moe
Molecules 2022, 27(13), 4270; https://0-doi-org.brum.beds.ac.uk/10.3390/molecules27134270 - 02 Jul 2022
Cited by 2 | Viewed by 1390
Abstract
Endonuclease III (EndoIII) is a bifunctional DNA glycosylase with specificity for a broad range of oxidized DNA lesions. The genome of an extremely radiation- and desiccation-resistant bacterium, Deinococcus radiodurans, possesses three genes encoding for EndoIII-like enzymes (DrEndoIII1, DrEndoIII2 and DrEndoIII3), which reveal [...] Read more.
Endonuclease III (EndoIII) is a bifunctional DNA glycosylase with specificity for a broad range of oxidized DNA lesions. The genome of an extremely radiation- and desiccation-resistant bacterium, Deinococcus radiodurans, possesses three genes encoding for EndoIII-like enzymes (DrEndoIII1, DrEndoIII2 and DrEndoIII3), which reveal different types of catalytic activities. DrEndoIII2 acts as the main EndoIII in this organism, while DrEndoIII1 and 3 demonstrate unusual and no EndoIII activity, respectively. In order to understand the role of DrEndoIII1 and DrEndoIII3 in D. radiodurans, we have generated mutants which target non-conserved residues in positions considered essential for classic EndoIII activity. In parallel, we have substituted residues coordinating the iron atoms in the [4Fe-4S] cluster in DrEndoIII2, aiming at elucidating the role of the cluster in these enzymes. Our results demonstrate that the amino acid substitutions in DrEndoIII1 reduce the enzyme activity without altering the overall structure, revealing that the residues found in the wild-type enzyme are essential for its unusual activity. The attempt to generate catalytic activity of DrEndoIII3 by re-designing its catalytic pocket was unsuccessful. A mutation of the iron-coordinating cysteine 199 in DrEndoIII2 appears to compromise the structural integrity and induce the formation of a [3Fe-4S] cluster, but apparently without affecting the activity. Taken together, we provide important structural and mechanistic insights into the three EndoIIIs, which will help us disentangle the open questions related to their presence in D. radiodurans and their particularities. Full article
(This article belongs to the Special Issue Metalloenzyme Biogenesis and Biocatalysis)
►▼ Show Figures

Figure 1

Review

Jump to: Research

15 pages, 1891 KiB  
Review
The Intriguing mitoNEET: Functional and Spectroscopic Properties of a Unique [2Fe-2S] Cluster Coordination Geometry
by Francesca Camponeschi, Mario Piccioli and Lucia Banci
Molecules 2022, 27(23), 8218; https://0-doi-org.brum.beds.ac.uk/10.3390/molecules27238218 - 25 Nov 2022
Cited by 7 | Viewed by 5862
Abstract
Despite the number of cellular and pathological mitoNEET-related processes, very few details are known about the mechanism of action of the protein. The recently discovered existence of a link between NEET proteins and cancer pave the way to consider mitoNEET and its Fe-S [...] Read more.
Despite the number of cellular and pathological mitoNEET-related processes, very few details are known about the mechanism of action of the protein. The recently discovered existence of a link between NEET proteins and cancer pave the way to consider mitoNEET and its Fe-S clusters as suitable targets to inhibit cancer cell proliferation. Here, we will review the variety of spectroscopic techniques that have been applied to study mitoNEET in an attempt to explain the drastic difference in clusters stability and reactivity observed for the two redox states, and to elucidate the cellular function of the protein. In particular, the extensive NMR assignment and the characterization of first coordination sphere provide a molecular fingerprint helpful to assist the design of drugs able to impair cellular processes or to directly participate in redox reactions or protein–protein recognition mechanisms. Full article
(This article belongs to the Special Issue Metalloenzyme Biogenesis and Biocatalysis)
►▼ Show Figures

Graphical abstract

17 pages, 1867 KiB  
Review
Repair of Iron Center Proteins—A Different Class of Hemerythrin-like Proteins
by Liliana S. O. Silva, Pedro M. Matias, Célia V. Romão and Lígia M. Saraiva
Molecules 2022, 27(13), 4051; https://0-doi-org.brum.beds.ac.uk/10.3390/molecules27134051 - 23 Jun 2022
Cited by 1 | Viewed by 1762
Abstract
Repair of Iron Center proteins (RIC) form a family of di-iron proteins that are widely spread in the microbial world. RICs contain a binuclear nonheme iron site in a four-helix bundle fold, two basic features of hemerythrin-like proteins. In this work, we review [...] Read more.
Repair of Iron Center proteins (RIC) form a family of di-iron proteins that are widely spread in the microbial world. RICs contain a binuclear nonheme iron site in a four-helix bundle fold, two basic features of hemerythrin-like proteins. In this work, we review the data on microbial RICs including how their genes are regulated and contribute to the survival of pathogenic bacteria. We gathered the currently available biochemical, spectroscopic and structural data on RICs with a particular focus on Escherichia coli RIC (also known as YtfE), which remains the best-studied protein with extensive biochemical characterization. Additionally, we present novel structural data for Escherichia coli YtfE harboring a di-manganese site and the protein’s affinity for this metal. The networking of protein interactions involving YtfE is also described and integrated into the proposed physiological role as an iron donor for reassembling of stress-damaged iron-sulfur centers. Full article
(This article belongs to the Special Issue Metalloenzyme Biogenesis and Biocatalysis)
►▼ Show Figures

Figure 1

Show export options expand_more Show export options expand_less
Select all
Export citation of selected articles as:
 
Displaying articles 1-4
Back to TopTop