Spectroscopic analysis of protein Fe-NO complexes.

Cesar Bellota-Anton, John Munnoch, Kirsty Robb, Katrin Adamczyk, Marco Candelaresi, Anthony W. Parker, Ray Dixon, Matthew I. Hutchings, Neil Hunt, Nicholas Tucker

Research output: Contribution to journalArticle

12 Citations (Scopus)


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.
Original languageEnglish
Pages (from-to)1293 -1298
Number of pages6
JournalBiochemical Society Transactions
Early online date21 Sep 2011
Publication statusPublished - 2011


  • spectroscopic analysis
  • protein
  • nitric oxide
  • free radical
  • iron nitrosyl complexes
  • TIC - Bionanotechnology

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  • Activities

    • 1 Key-note speaker and plenary lectures at conferences

    Analysis of free radicals, radical modifications and redox signalling

    Nicholas Tucker (Invited speaker)

    18 Apr 201119 Apr 2011

    Activity: Participating in or organising an event typesKey-note speaker and plenary lectures at conferences

    Cite this

    Bellota-Anton, C., Munnoch, J., Robb, K., Adamczyk, K., Candelaresi, M., Parker, A. W., Dixon, R., Hutchings, M. I., Hunt, N., & Tucker, N. (2011). Spectroscopic analysis of protein Fe-NO complexes. Biochemical Society Transactions, 39, 1293 -1298. https://doi.org/10.1042/BST0391293