The toxic free radical NO (nitric oxide) has diverse biological roles in eukaryotes and bacteria, being involved in signalling, vasodilation, blood clotting and immunity, and as an intermediate in microbial denitrification. The predominant biological mechanism of detecting NO is through the formation of iron nitrosyl complexes, although this is a deleterious process for other iron-containing enzymes. We have previously applied techniques such as UV–visible and EPR spectroscopy to the analysis of protein Fe–NO complex formation in order to study how NO controls the activity of the bacterial transcriptional regulators NorR and NsrR. These studies have analysed NO-dependent biological activity both in vitro and in vivo using diverse biochemical, molecular and spectroscopic methods. Recently, we have applied ultrafast 2D-IR (two-dimensional IR) spectroscopy to the analysis of NO–protein interactions using Mb (myoglobin) and Cc (cytochrome c) as model haem proteins. The ultrafast fluctuations of Cc and Mb show marked differences, indicating altered flexibility of the haem pockets. We have extended this analysis to bacterial catalase enzymes that are known to play a role in the nitrosative stress response by detoxifying peroxynitrite. The first 2D-IR analysis of haem nitrosylation and perspectives for the future are discussed.
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October 2011
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Conference Article|
September 21 2011
Spectroscopic analysis of protein Fe–NO complexes
César Bellota-Antón;
César Bellota-Antón
*Strathclyde Institute for Pharmaceutical and Biomedical Sciences, University of Strathclyde, 161 Cathedral Street, Glasgow G4 ORE, U.K.
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John Munnoch;
John Munnoch
*Strathclyde Institute for Pharmaceutical and Biomedical Sciences, University of Strathclyde, 161 Cathedral Street, Glasgow G4 ORE, U.K.
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Kirsty Robb;
Kirsty Robb
*Strathclyde Institute for Pharmaceutical and Biomedical Sciences, University of Strathclyde, 161 Cathedral Street, Glasgow G4 ORE, U.K.
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Katrin Adamczyk;
Katrin Adamczyk
†Department of Physics, University of Strathclyde, SUPA, 107 Rottenrow East, Glasgow G4 ONG, U.K.
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Marco Candelaresi;
Marco Candelaresi
†Department of Physics, University of Strathclyde, SUPA, 107 Rottenrow East, Glasgow G4 ONG, U.K.
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Anthony W. Parker;
Anthony W. Parker
‡Central Laser Facility, Research Complex at Harwell, STFC Rutherford Appleton Laboratory, Harwell Oxford, Didcot, Oxon OX11 0QX, U.K.
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Ray Dixon;
Ray Dixon
§Department of Molecular Microbiology, John Innes Centre, Norwich Research Park, Colney, Norwich NR4 7UH, U.K.
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Matthew I. Hutchings;
Matthew I. Hutchings
‖School of Biological Sciences, University of East Anglia, Norwich Research Park, Colney, Norwich NR4 7TJ, U.K.
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Neil T. Hunt;
Neil T. Hunt
†Department of Physics, University of Strathclyde, SUPA, 107 Rottenrow East, Glasgow G4 ONG, U.K.
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Nicholas P. Tucker
Nicholas P. Tucker
1
*Strathclyde Institute for Pharmaceutical and Biomedical Sciences, University of Strathclyde, 161 Cathedral Street, Glasgow G4 ORE, U.K.
1To whom correspondence should be addressed (email nick.tucker@strath.ac.uk).
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Publisher: Portland Press Ltd
Received:
June 03 2011
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© The Authors Journal compilation © 2011 Biochemical Society
2011
Biochem Soc Trans (2011) 39 (5): 1293–1298.
Article history
Received:
June 03 2011
Citation
César Bellota-Antón, John Munnoch, Kirsty Robb, Katrin Adamczyk, Marco Candelaresi, Anthony W. Parker, Ray Dixon, Matthew I. Hutchings, Neil T. Hunt, Nicholas P. Tucker; Spectroscopic analysis of protein Fe–NO complexes. Biochem Soc Trans 1 October 2011; 39 (5): 1293–1298. doi: https://doi.org/10.1042/BST0391293
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