Design Strategies for Redox Active Metalloenzymes: Applications in Hydrogen Production

R. Alcala-Torano, D. J. Sommer, Z. Bahrami Dizicheh, Giovanna Ghirlanda

Research output: Chapter in Book/Report/Conference proceedingChapter

3 Scopus citations


The last decades have seen an increased interest in finding alternative means to produce renewable fuels in order to satisfy the growing energy demands and to minimize environmental impact. Nature can serve as an inspiration for development of these methodologies, as enzymes are able to carry out a wide variety of redox processes at high efficiency, employing a wide array of earth-abundant transition metals to do so. While it is well recognized that the protein environment plays an important role in tuning the properties of the different metal centers, the structure/function relationships between amino acids and catalytic centers are not well resolved. One specific approach to study the role of proteins in both electron and proton transfer is the biomimetic design of redox active peptides, binding organometallic clusters in well-understood protein environments. Here we discuss different strategies for the design of peptides incorporating redox active FeS clusters, [FeFe]-hydrogenase organometallic mimics, and porphyrin centers into different peptide and protein environments in order to understand natural redox enzymes.

Original languageEnglish (US)
Title of host publicationMethods in Enzymology
PublisherAcademic Press Inc
Number of pages28
StatePublished - 2016

Publication series

NameMethods in Enzymology
ISSN (Print)0076-6879
ISSN (Electronic)1557-7988


  • Artificial enzymes
  • Artificial hydrogenases
  • Carbon dioxide reduction
  • De novo design
  • Hydrogen production
  • Iron–sulfur clusters
  • Metalloproteins
  • Porphyrin-binding proteins

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology


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