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Resources

Welcome to the ELEMENTAL Hub Resources page, your central destination for key documents, guidance, and materials related to our research.

Here you’ll find information to support collaboration, project development, and knowledge exchange across the Hub. Whether you’re a researcher, industry partner, or stakeholder, these resources are designed to help you navigate our programmes, understand our focus areas, and engage with the work we’re doing to develop sustainable solutions for metal recovery and reuse.

Publications and Papers

Drs Louise Byfield and Sigrid Kusch-Brandt from the Environmental Biotechnology Network have published an anthology of short stories related to Environmental Biotechnology. You can read it here: Green stories: microbes to the rescue! 

Peter T. Chivers, Priyanka Basak, and Michael J. Maroney have published a paper on the overlooked role of low molecular weight metal–ligand complexes, particularly L-histidine, in microbial nickel uptake, gene expression, and metalloenzyme maturation. This review explores the coordination chemistry of Ni(II)–histidine complexes and their fundamental importance to cellular metal homeostasis.

Highlights:

  • Low molecular weight metal complexes play important roles in many physiological processes.
  • L-His is a component of cytosolic metal buffers with which other biomolecules compete.
  • At cellular Ni and L-His concentrations, Ni(His)+ and Ni(His)2 both play roles.
  • Ternary complexes are important for buffering, homeostasis, and enzyme maturation.

https://doi.org/10.1016/j.jinorgbio.2024.112668 

Abstract
Biological environments present a complex array of metal-binding ligands. Metal-binding proteins have been the overwhelming focus of study because of their important and well-defined biological roles. Consequently, the presence of functional low molecular weight (LMW) metal-ligand complexes has been overlooked in terms of their roles in metallobiochemistry, particularly within cells. Recent studies in microbial systems have illuminated the different roles of L-histidine in nickel uptake, gene expression, and metalloenzyme maturation. In this focused critical review, these roles are surveyed in the context of the coordination chemistry of Ni(II) ions and the amino acid histidine, and the physico-chemical properties of nickel complexes of histidine. These complexes are fundamentally important to cellular metal homeostasis and further work is needed to fully define their contributions.

Researchers at the University of Durham have made an exciting discovery that could revolutionise how scientists design and engineer biological systems.

Their new study reveals a way to predict and control how proteins inside cells bind to metals – an essential process for life.

Revealing secrets of protein metalation

Metals such as iron, manganese, and cobalt are crucial for many biological processes, helping proteins carry out vital functions in cells.

However, scientists have long struggled to understand how proteins select the right metal inside cells.

Now, the research team have found a way to solve this problem using a special protein that acts as a metal trap.

This protein, originally found in cyanobacteria (a type of photosynthetic bacteria), naturally binds to manganese.

By studying how it interacts with different metals, the researchers have demonstrated that they can accurately predict which metals proteins will bind to in various environments.

This discovery is important because when proteins are introduced into cells with different metal levels, they can sometimes bind to the wrong metal, which may impact their function.

Metalation calculator

To help address this challenge, the researchers have developed a tool called a metalation calculator, which uses data from the cells’ own metal sensors to predict how proteins will behave.

In their experiments, they found that when the manganese-binding protein was placed inside E. coli bacteria, it mistakenly bound to iron instead of manganese.

This highlights the need to carefully control metal availability when designing biological systems.

This research opens exciting possibilities for creating biological systems that work more efficiently and sustainably. It’s a big step forward for fields such as medicine, environmental science, and sustainable manufacturing.

The findings have significant applications for industries that rely on engineered biological processes, such as pharmaceutical development, industrial enzyme production, and green technologies.

This research was made possible thanks to funding from UK Research and Innovation (UKRI) and Biotechnology and Biological Sciences Research Council (BBSRC), which have supported the team’s work on metals in biology for over 40 years.

Dr Natalie Byrd and colleagues latest study, shows how a common environmental bacterium, Shewanella oneidensis, can turn dissolved copper into useful nanoparticles. We found that a specific enzyme, known as HyaB (a [NiFe] hydrogenase), uses hydrogen to drive this transformation, helping the cells convert copper ions into stable copper nanoparticles. The process happens during anaerobic respiration, where the bacteria oxidise hydrogen via HyaB to release electrons, and those electrons are then used to reduce copper. By combining targeted gene knockouts, aqueous chemical analysis, and high-resolution electron microscopy, we linked HyaB activity directly to nanoparticle formation and visualised their production in the periplasm. Remarkably, the particles proved effective as catalysts in “click chemistry” reactions, showing how microbes could help us both clean up liquid wastes containing copper and create valuable new materials in a sustainable way. Looking ahead, this work can be used as a template for using engineering biology to enhance and fine-tune microbes for the tailored production of nanomaterials.

Abstract:

Shewanella oneidensis MR-1 can biosynthesize cell-supported Cu-nanoparticles (CuNPs), via the bioreduction of Cu(II)(aq), with excellent catalytic activity for click chemistry reactions. However, enzymatic mechanisms underpinning Cu(II) bioreduction were unclear. Here, the oxidation of hydrogen as electron donor was essential for Cu(II) bioreduction by S. oneidensis and hydrogenase deletion mutants were used to demonstrate the critical role of the periplasmic [NiFe] hydrogenase, HyaB. Wild type (WT) cultured cells coupled hydrogen oxidation to biosynthesis of Cu(0)/Cu(I)-NPs within the periplasm (identified using XRD and TEM with SAED, EDS, EELS); ΔhyaB mutants did not produce CuNPs. Biosynthesized CuNPs were catalytically active for the cycloaddition of methyl azidoacetate and 1-hexyne, confirming the potential for microbial revalorization of Cu(II)-containing wastewaters, by forming catalytically active nanomaterials. Identifying HyaB, as a key mediator for Cu(II) reduction in S. oneidensis is an important first step towards developing industrial bioprocesses for Cu(II) recovery and CuNP synthesis, offering a template for improvements using engineering biology. Interestingly, c-type cytochromes, critical for reduction of other metals, were unable to fully reduce Cu(II)(aq) in vivo despite being capable of Cu(II) reduction under in vitro conditions. In fact, Cu inhibited outer membrane cytochrome mediated reduction of Pd(II), and this may impact bioreduction of mixed metal solutions/effluents.

Byrd, N., Egan Morriss, C., Parker, J., Cai, R., Nunn, E. J., van Wonderen, J. H., Cavet, J. S., Parmeggiani, F., Kimber, R. L., Gralnick, J. A., Clarke, T. A., Haigh, S. J., & Lloyd, J. R. (2025). Hydrogenase Mediated Biosynthesis of Catalytically Active Cu Nanoparticles. Small, Article 2500210. Advance online publication. https://doi.org/10.1002/smll.202500210

Full publication here. 

Tools and Metrics

Professor Paul Freemont recently Chaired a Task Force which identified key priority areas for standards and metrics development in engineering biology. Their report may be found here.

 

A more extensive and user friendly “Metalation Calculator II” has been released based on data from a new paper. Find the “Metalation Calculator II” on the E3B BBSRC NIBB website.

Brunswick Confidentiality agreements for 2 and 3 parties. Please note that your home institution and any industrial collaborator will both need to approve this.

Confidentiality-Agreement-2-way

Confidentiality-Agreement-3-way

Here you can access a selection of Elemental logos, available for use in publications, presentations, posters, and other relevant materials.

If you plan to use the Elemental logo in any of your work, please let the Elemental Hub team know by sending an email to elementalmetalhub@kent.ac.uk. This helps us track usage and ensure consistent branding across all communications.

If you require the logo in a different format or have any questions, feel free to get in touch.

  • Elemental Dark Logo
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  • Elemental All Black Logo

 

Elemental offers letters of support to our members who are applying for grants or funding opportunities related to metal recovery, engineering biology, and other aligned research areas. These letters can help strengthen your application by demonstrating institutional backing and alignment with Elemental’s mission.

If you are a member and would like to request a letter of support, please get in touch with us at elementalmetalhub@kent.ac.uk with details of your proposal, the funding body, and any relevant deadlines.

We recommend contacting us as early as possible to allow sufficient time for review and preparation of your letter.