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Comparative studies of soluble and immobilized Fe(III) heme-peptide complexes as alternative heterogeneous biocatalysts

  • Joey Lukas , Ivona Družeta and Toni Kühl ORCID logo EMAIL logo
Published/Copyright: October 19, 2022
Biological Chemistry
From the journal Biological Chemistry Volume 403 Issue 11-12

Abstract

Fe(III) heme is known to possess low catalytic activity when exposed to hydrogen peroxide and a reducing substrate. Efficient non-covalently linked Fe(III) heme-peptide complexes may represent suitable alternatives as a new group of green catalysts. Here, we evaluated a set of heme-peptide complexes by determination of their peroxidase-like activity and the kinetics of the catalytic conversion in both, the soluble and the immobilized state. We show the impact of peptide length on binding of the peptides to Fe(III) heme and the catalytic activity. Immobilization of the peptide onto a polymer support maintains the catalytic performance of the Fe(III) heme-peptide complex. This study thus opens up a new perspective with regard to the development of heterogeneous biocatalysts with a peroxidase-like activity.

Keywords: biocatalyst; heme; heterogeneous catalysis; peptide; peroxidase-like activity
Corresponding author: Toni Kühl, Pharmaceutical Biochemistry and Bioanalytics, Pharmaceutical Institute, University of Bonn, An der Immenburg 4, D-53121, Bonn, Germany, E-mail:
Joey Lukas and Ivona Družeta contributed equally to this work.

Funding source: Rheinische Friedrich-Wilhelms-Universität Bonn

Acknowledgments

We would like to acknowledge technical support by Maximilian Steve Beck, Sonali Vaidya and Clemens Peiter. Provision of trifluoroacetic acid by Solvay GmbH (Hannover, Germany) is kindly acknowledged. Also, we would like to express our gratitude to Prof. Diana Imhof for access to facilities and instruments in the department of Pharmaceutical Biochemistry and Bioanalytics, University of Bonn.

  1. Author contributions: All the authors have accepted responsibility for the entire content of this submitted manuscript and approved submission.

  2. Research funding: Financial support by the University of Bonn is greatly acknowledged.

  3. Conflict of interest statement: The authors declare no conflicts of interest regarding this article.

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Supplementary Material

The online version of this article offers supplementary material (https://doi.org/10.1515/hsz-2022-0199).

Received: 2022-06-06
Accepted: 2022-10-06
Published Online: 2022-10-19
Published in Print: 2022-11-25

© 2022 Walter de Gruyter GmbH, Berlin/Boston

Articles in the same Issue

  1. Frontmatter
  2. Heme research – the past, the present and the future
  3. A primer on heme biosynthesis
  4. New roles for GAPDH, Hsp90, and NO in regulating heme allocation and hemeprotein function in mammals
  5. The role of host heme in bacterial infection
  6. Signal transduction mechanisms in heme-based globin-coupled oxygen sensors with a focus on a histidine kinase (AfGcHK) and a diguanylate cyclase (YddV or EcDosC)
  7. Heme delivery to heme oxygenase-2 involves glyceraldehyde-3-phosphate dehydrogenase
  8. Novel insights into heme binding to hemoglobin
  9. Extracellular hemin is a reverse use-dependent gating modifier of cardiac voltage-gated Na+ channels
  10. Assessment of the breadth of binding promiscuity of heme towards human proteins
  11. Determination of free heme in stored red blood cells with an apo-horseradish peroxidase-based assay
  12. Comparative studies of soluble and immobilized Fe(III) heme-peptide complexes as alternative heterogeneous biocatalysts
https://doi.org/10.1515/hsz-2022-0199
Keywords for this article
biocatalyst; heme; heterogeneous catalysis; peptide; peroxidase-like activity

Articles in the same Issue

  1. Frontmatter
  2. Heme research – the past, the present and the future
  3. A primer on heme biosynthesis
  4. New roles for GAPDH, Hsp90, and NO in regulating heme allocation and hemeprotein function in mammals
  5. The role of host heme in bacterial infection
  6. Signal transduction mechanisms in heme-based globin-coupled oxygen sensors with a focus on a histidine kinase (AfGcHK) and a diguanylate cyclase (YddV or EcDosC)
  7. Heme delivery to heme oxygenase-2 involves glyceraldehyde-3-phosphate dehydrogenase
  8. Novel insights into heme binding to hemoglobin
  9. Extracellular hemin is a reverse use-dependent gating modifier of cardiac voltage-gated Na+ channels
  10. Assessment of the breadth of binding promiscuity of heme towards human proteins
  11. Determination of free heme in stored red blood cells with an apo-horseradish peroxidase-based assay
  12. Comparative studies of soluble and immobilized Fe(III) heme-peptide complexes as alternative heterogeneous biocatalysts
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