Recent Insights into Metal Binding Proteins

Dear Colleagues,

Metal ions impart important functional and structural diversity to biologic systems. Without metal ions, biochemical processes would be impossible. Only the elemental characteristics of metal ions can support life’s diverse needs in terms of on redox chemistry, energy transduction, molecular transport, cellular detoxification, protection, regulation, and signaling.

Currently, more than 40% of all known protein structures contain metal ions, with characteristic structures ranging from simple mononuclear bound atoms to complex multi- or hetero-metal clusters. With only a handful of amino acids, organic cofactors, small molecules and labile atoms known to contribute metal ion binding in proteins, the known structural plasticity is surprising. Tailored by evolution, binding sites are strongholds that address catalysis or fleeting when metal transport is needed.

Dealing with metal ions also requires us to find solutions that an avoid availability and toxicity problems. Enzymes that contribute to homeostasis are certainly among the most ubiquitous systems in biology. Excellent examples include the protein nanocages that deal with iron storage and the toxicity that can be found to possess the same basic structural features and functions in all living organisms.

This Special Issue aims to publish up-to-date views and highlight recent discoveries in the structural and functional characterization of metal-binding proteins structural and their impact on biology. As such, we would like to invite experts in the field to contribute both original research papers and review articles, covering basic aspects and future directions in the field.

Dr. Pedro Tavares
Dr. Alice S. Pereira
Guest Editors

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