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Special Issue "Thiophilic Metals: An Ancient Love for Sulfur at the Heart of Biochemistry"

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

Deadline for manuscript submissions: 31 July 2021.

Special Issue Editors

Prof. Dr. Claus Jacob
Website
Guest Editor
Division of Bioorganic Chemistry, School of Pharmacy, Saarland University, D-66123 Saarbruecken, Germany
Interests: bioorganic chemistry; catalytic sensor/effector agents; epistemology; intracellular diagnostics; nanotechnology; natural products; reactive sulfur and selenium species; redox regulation via the cellular thiolstat
Special Issues and Collections in MDPI journals
Prof. Dr. Wolfgang Maret
Website
Guest Editor
Departments of Biochemistry and Nutritional Sciences, King’s College London, 150 Stamford Street, London SE1 9NH, United Kingdom

Special Issue Information

Dear Colleagues,

Thiophilic metal ions, such as zinc, copper, iron, and molybdenum, are present in virtually all organisms where they fulfil a multitude of functions and often bind to sulfur as their ligands. The resulting medley of metal binding and exchange on the one side and redox activity of some of these metals and sulfur ligands on the other leads to a truly complex chemistry that is reflected in their biochemistry. This Special Issue will consider the current state of such thiophilic metal ions in biology, with a focus on their chemistry, trafficking, exchange, biological actions, and redox control. Some of this bioinorganic chemistry is established, other aspects are still speculative and in need of investigation. This includes evolutionary aspects; sulfur cycles controlling such thiophilic metals in the geosphere and biosphere; and selenophilic metals and interactions with other chalcogens, such as tellurium and polonium. This Special Issue is dedicated to Bert L. Vallee, the discoverer of the metallothioneins, on occasion of his 100th birthday in 2019.

Prof. Dr. Claus Jacob
Prof. Dr. Wolfgang Maret
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 papers will be 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.

Published Papers (1 paper)

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Research

Open AccessArticle
Characterization and Reconstitution of Human Lipoyl Synthase (LIAS) Supports ISCA2 and ISCU as Primary Cluster Donors and an Ordered Mechanism of Cluster Assembly
Int. J. Mol. Sci. 2021, 22(4), 1598; https://0-doi-org.brum.beds.ac.uk/10.3390/ijms22041598 - 05 Feb 2021
Abstract
Lipoyl synthase (LIAS) is an iron–sulfur cluster protein and a member of the radical S-adenosylmethionine (SAM) superfamily that catalyzes the final step of lipoic acid biosynthesis. The enzyme contains two [4Fe–4S] centers (reducing and auxiliary clusters) that promote radical formation and sulfur transfer, [...] Read more.
Lipoyl synthase (LIAS) is an iron–sulfur cluster protein and a member of the radical S-adenosylmethionine (SAM) superfamily that catalyzes the final step of lipoic acid biosynthesis. The enzyme contains two [4Fe–4S] centers (reducing and auxiliary clusters) that promote radical formation and sulfur transfer, respectively. Most information concerning LIAS and its mechanism has been determined from prokaryotic enzymes. Herein, we detail the expression, isolation, and characterization of human LIAS, its reactivity, and evaluation of natural iron–sulfur (Fe–S) cluster reconstitution mechanisms. Cluster donation by a number of possible cluster donor proteins and heterodimeric complexes has been evaluated. [2Fe–2S]-cluster-bound forms of human ISCU and ISCA2 were found capable of reconstituting human LIAS, such that complete product turnover was enabled for LIAS, as monitored via a liquid chromatography–mass spectrometry (LC–MS) assay. Electron paramagnetic resonance (EPR) studies of native LIAS and substituted derivatives that lacked the ability to bind one or the other of LIAS’s two [4Fe–4S] clusters revealed a likely order of cluster addition, with the auxiliary cluster preceding the reducing [4Fe–4S] center. These results detail the trafficking of Fe–S clusters in human cells and highlight differences with respect to bacterial LIAS analogs. Likely in vivo Fe–S cluster donors to LIAS are identified, with possible connections to human disease states, and a mechanistic ordering of [4Fe–4S] cluster reconstitution is evident. Full article
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