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Metalloenzyme

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 (31 May 2018) | Viewed by 4927

Special Issue Editor


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Guest Editor
Department of Chemistry, Keio University 3-14-1 Hiyoshi, Yokohama, Kanagawa 223-8522, Japan
Interests: metalloprotein; Cu/Zn-superoxide dismutase; metallochaperone; neurodegenerative disease; amyotrophic lateral sclerosis

Special Issue Information

Dear Colleagues,

Metalloenzymes are proteins that bind heavy metal ions as active sites for enzymatic reactions and/or structural factors regulating protein stabilities. In many physiological processes, metalloenzymes play central roles, which are substantiated by the estimation that around 30% of the proteome are proteins binding heavy metal ions. In spite of structural, as well as functional, requirements of metal ions for metalloenzymes, heavy metal ions can exert toxicity: Indeed, there is no single metal ion (copper and zinc, in particular) that is freely available within cells. It is, hence, important to know how metal ions are delivered correctly to metal-requiring proteins in cells. Furthermore, functional and metabolic breakdowns of metalloenzymes are related to various diseases including anemia, neurodegenerative disorders, cancer, and diabetes, which further points to the relevance of metalloenzymes in our lives.

This Special Issue on “Metalloenzymes” will be comprised of original research papers and reviews covering various aspects of metalloenzymes. Contributions from research on the structure–function relationships of metalloenzymes and intracellular metabolism of heavy metal ions will be welcome. Studies on pathological roles of heavy metal ions and metalloenzymes will also be considered.

Dr. Yoshiaki Furukawa
Guest Editor

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Keywords

  • metalloenzyme
  • metalloprotein
  • metallochaperone
  • intracellular metal ion
  • protein structure
  • protein-protein interaction
  • heavy metal toxicity
  • neurodegenerative disease

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Published Papers (1 paper)

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Research

17 pages, 1683 KiB  
Article
Artificial Heme Enzymes for the Construction of Gold-Based Biomaterials
by Gerardo Zambrano, Emmanuel Ruggiero, Anna Malafronte, Marco Chino, Ornella Maglio, Vincenzo Pavone, Flavia Nastri and Angela Lombardi
Int. J. Mol. Sci. 2018, 19(10), 2896; https://doi.org/10.3390/ijms19102896 - 24 Sep 2018
Cited by 18 | Viewed by 4486
Abstract
Many efforts are continuously devoted to the construction of hybrid biomaterials for specific applications, by immobilizing enzymes on different types of surfaces and/or nanomaterials. In addition, advances in computational, molecular and structural biology have led to a variety of strategies for designing and [...] Read more.
Many efforts are continuously devoted to the construction of hybrid biomaterials for specific applications, by immobilizing enzymes on different types of surfaces and/or nanomaterials. In addition, advances in computational, molecular and structural biology have led to a variety of strategies for designing and engineering artificial enzymes with defined catalytic properties. Here, we report the conjugation of an artificial heme enzyme (MIMO) with lipoic acid (LA) as a building block for the development of gold-based biomaterials. We show that the artificial MIMO@LA can be successfully conjugated to gold nanoparticles or immobilized onto gold electrode surfaces, displaying quasi-reversible redox properties and peroxidase activity. The results of this work open interesting perspectives toward the development of new totally-synthetic catalytic biomaterials for application in biotechnology and biomedicine, expanding the range of the biomolecular component aside from traditional native enzymes. Full article
(This article belongs to the Special Issue Metalloenzyme)
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