ArticleProceedings of the National Academy of Sciences of the United States of America2008
Zinc porphyrin: a fluorescent acceptor in studies of Zn-cytochrome c unfolding by fluorescence resonance energy transfer.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Oleoyl coenzyme A triggers peroxygenase activity in cytochrome c.Journal of inorganic biochemistry · 2026Article
- Deducing the conformational space for an octa-proline helix.Chemical science · 2024Article
- Ligand-binding assay based on microfluidic chemotaxis of porphyrin receptors.Chemical science · 2022Article
- The Human CytochromeBiochemistry · 2020Article
- Structure of a Zinc Porphyrin-Substituted Bacterioferritin and Photophysical Properties of Iron Reduction.Biochemistry · 2020Article
- The Periodic Table's Impact on Bioinorganic Chemistry and Biology's Selective Use of Metal Ions.Structure and bonding · 2019Article
- Design of artificial metalloproteins/metalloenzymes by tuning noncovalent interactions.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Review
- Structural transformations of cytochrome c upon interaction with cardiolipin.Chemistry and physics of lipids · 2014Review
- Exceptionally stable, redox-active supramolecular protein assemblies with emergent properties.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Becoming a peroxidase: cardiolipin-induced unfolding of cytochrome c.The journal of physical chemistry. B · 2013Article
- Single-Molecule Analysis of CytochromeThe journal of physical chemistry letters · 2013Article
- Origin of the conformational heterogeneity of cardiolipin-bound cytochrome C.Journal of the American Chemical Society · 2012Article
- Conformational properties of cardiolipin-bound cytochrome c.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Manifestations of native topology in the denatured state ensemble of Rhodopseudomonas palustris cytochrome c'.Biochemistry · 2011Article
- Thermodynamics of loop formation in the denatured state of rhodopseudomonas palustris cytochrome c': scaling exponents and the reconciliation problem.Journal of molecular biology · 2009Article
- Three-pulse photon echo peak shift spectroscopy as a probe of flexibility and conformational heterogeneity in protein folding.Chemical physics letters · 2009Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
FRET between the zinc porphyrin (ZnP) chromophore in zinc-substituted cytochrome c (Zn-cyt c) and an Alexa Fluor dye attached to specific surface sites was used to characterize Zn-cyt c unfolding. The use of ZnP as a fluorescent acceptor eliminates the need to doubly label the protein with exogenous dyes to perform FRET experiments in which both donor and acceptor fluorescence is monitored. The requirement for attachment of only one dye also minimizes perturbation to the protein. This sensitive technique allowed for the determination of distances between the label placed at six different sites and ZnP through a range of denaturant concentrations. Fitting of the data to a three-state model provides distances in the unfolding intermediate. The use of ZnP as a fluorescent acceptor of energy in FRET has a significant potential for application to a range of other systems including heme-binding proteins and proteins to which a covalently attached heme tag may be added.
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