ArticleMetallomics : integrated biometal science2011
2D-SEIRA spectroscopy to highlight conformational changes of the cytochrome c oxidase induced by direct electron transfer.
Article in Metallomics : integrated biometal science, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 18 citations in OpenAlex.
- Stimuli-Responsive Oligourea Molecular Films.ACS applied materials & interfaces · 2024Article
- Biomimetic Membranes for Multi-Redox Center Proteins.International journal of molecular sciences · 2016Review
- Time-resolved surface-enhanced IR-absorption spectroscopy of direct electron transfer to cytochrome c oxidase from R. sphaeroides.Biophysical journal · 2013Article
- Two-dimensional heterospectral correlation analysis of the redox-induced conformational transition in cytochrome c using surface-enhanced Raman and infrared absorption spectroscopies on a two-layer gold surface.The journal of physical chemistry. B · 2013Article
- From static structure to living protein: computational analysis of cytochrome c oxidase main-chain flexibility.Biophysical journal · 2012Article
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Authors and funding
8 authors at 5 institutions in 3 countries.
Funding
Abstract
Potentiometric titrations of the cytochrome c oxidase (CcO) immobilized in a biomimetic membrane system were followed by two-dimensional surface-enhanced IR absorption spectroscopy (2D SEIRAS) in the ATR-mode. Direct electron transfer was employed to vary the redox state of the enzyme. The CcO was shown to undergo a conformational transition from a non-activated to an activated state after it was allowed to turnover in the presence of oxygen. Differences between the non-activated and activated state were revealed by 2D SEIRA spectra recorded as a function of potential. The activated state was characterized by a higher number of correlated transitions as well as a higher number of amino acids associated with electron transfer.
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