Probing heavy metal binding to phycobiliproteins

Jeddidiah Bellamy-Carter; Jaspreet K Sound; Aneika C Leney

doi:10.1111/febs.16396

Probing heavy metal binding to phycobiliproteins

Jeddidiah Bellamy-Carter, Jaspreet K Sound, Aneika C Leney

Biosciences

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Abstract

Blue-green algae, also known as cyanobacteria, contain some of the most efficient light harvesting complexes known. These large, colourful complexes consist of phycobiliproteins which are extremely valuable in the cosmetics, food, nutraceutical and pharmaceutical industries. Additionally, the colourful and fluorescent properties of phycobiliproteins can be modulated by metal ions, making them highly attractive as heavy metal sensors and heavy metal scavengers. Although the overall quenching ability metal ions have on phycobiliproteins is known, the mechanism of heavy metal binding to phycobiliproteins is not fully understood, limiting their widespread quantitative applications. Here, we show using high-resolution native mass spectrometry that phycobiliprotein complexes bind metal ions in different manners. Through monitoring the binding equilibria and metal binding stoichiometry, we show in particular copper and silver to have drastic, yet different effects on phycobiliprotein structure, both copper and silver modulate the overall complex properties. Together, the data reveals the mechanisms by which metal ions can modulate phycobiliprotein properties which can be used as a basis for the future design of metal-related phycobiliprotein applications.

Original language	English
Pages (from-to)	4646-4656
Journal	The FEBS journal
Volume	289
Issue number	15
Early online date	14 Feb 2022
DOIs	https://doi.org/10.1111/febs.16396
Publication status	E-pub ahead of print - 14 Feb 2022

Bibliographical note

Funding Information:
We are extremely thankful for Dr David H. Green at the Scottish Association for Marine Science, and Cecilia Rad‐Menendez and Karen MacKechnie at the Culture Collection of Algae and Protozoa (CCAP) for providing algae cultures and for their help and advice with maintaining the algae. We thank Dr Todd Mize for critical reading of this manuscript and Alexandra Munro‐Clark for preliminary purification experiments. JBC, JS and ACL were funded through a BBSRC grant (BB/T015640/1). Funding for reagents and consumables was provided jointly by BBSRC (BB/T015640/1), The Royal Society (RGS\R1\201411) and the University of Birmingham. The Orbitrap Eclipse mass spectrometer used in this research was funded by the BBSRC (BB/S019456/1). We acknowledge the Advanced Mass Spectrometry Facility at the University of Birmingham for maintenance of the instruments used in this study.

Publisher Copyright:
© 2022 The Authors. The FEBS Journal published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies

Keywords

heavy metal toxicity
light-harvesting complex
native mass spectrometry
phycobiliproteins
protein-metal interactions

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

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The phycobilisome; how can light energy be converted to chemical energy with 95% efficiency?
Leney, A.
Biotechnology & Biological Sciences Research Council
1/10/20 → 31/12/24
Project: Research Councils
A new mass spectrometer for structural proteomics and protein imaging
Thomas, C., Grant, M., Lovering, A., Alderwick, L., Tomlinson, M., Winn, P., Knowles, T., Cooper, H., Styles, I., Gibbs, D., Huber, D., Bhatt, A. & Leney, A.
Biotechnology & Biological Sciences Research Council
1/07/19 → 30/06/20
Project: Research

Research data supporting "Probing heavy metal binding to phycobiliproteins"
Bellamy-Carter, J. (Creator), Sound, J. (Creator) & Leney, A. (Creator), University of Birmingham, 2 Feb 2022
DOI: 10.25500/edata.bham.00000780
Dataset

Cite this

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abstract = "Blue-green algae, also known as cyanobacteria, contain some of the most efficient light harvesting complexes known. These large, colourful complexes consist of phycobiliproteins which are extremely valuable in the cosmetics, food, nutraceutical and pharmaceutical industries. Additionally, the colourful and fluorescent properties of phycobiliproteins can be modulated by metal ions, making them highly attractive as heavy metal sensors and heavy metal scavengers. Although the overall quenching ability metal ions have on phycobiliproteins is known, the mechanism of heavy metal binding to phycobiliproteins is not fully understood, limiting their widespread quantitative applications. Here, we show using high-resolution native mass spectrometry that phycobiliprotein complexes bind metal ions in different manners. Through monitoring the binding equilibria and metal binding stoichiometry, we show in particular copper and silver to have drastic, yet different effects on phycobiliprotein structure, both copper and silver modulate the overall complex properties. Together, the data reveals the mechanisms by which metal ions can modulate phycobiliprotein properties which can be used as a basis for the future design of metal-related phycobiliprotein applications.",

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note = "Funding Information: We are extremely thankful for Dr David H. Green at the Scottish Association for Marine Science, and Cecilia Rad‐Menendez and Karen MacKechnie at the Culture Collection of Algae and Protozoa (CCAP) for providing algae cultures and for their help and advice with maintaining the algae. We thank Dr Todd Mize for critical reading of this manuscript and Alexandra Munro‐Clark for preliminary purification experiments. JBC, JS and ACL were funded through a BBSRC grant (BB/T015640/1). Funding for reagents and consumables was provided jointly by BBSRC (BB/T015640/1), The Royal Society (RGS\R1\201411) and the University of Birmingham. The Orbitrap Eclipse mass spectrometer used in this research was funded by the BBSRC (BB/S019456/1). We acknowledge the Advanced Mass Spectrometry Facility at the University of Birmingham for maintenance of the instruments used in this study. Publisher Copyright: {\textcopyright} 2022 The Authors. The FEBS Journal published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies",

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Probing heavy metal binding to phycobiliproteins

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

Access to Document

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Projects

The phycobilisome; how can light energy be converted to chemical energy with 95% efficiency?

A new mass spectrometer for structural proteomics and protein imaging

Datasets

Research data supporting "Probing heavy metal binding to phycobiliproteins"

Cite this