title: Direct conversion of cytochrome c spectral shifts to fluorescence using photochromic FRET.
abstract: Photochromic fluorescence resonance energy transfer (pcFRET) was used to monitor the redox activity of non-fluorescent heme protein. Venus fluorescent protein was used as a donor where its emission intensity was reversibly modulated by the absorption change of Cytochrome c.
authors.affiliation: Department of Chemical and Biological Engineering, Koc University, Istanbul, 34450, Turkey.
authors.forename: Selen
authors.initials: S
authors.lastname: Manioglu
authors.forename: Muge
authors.initials: M
authors.lastname: Atis
authors.forename: Mehdi
authors.initials: M
authors.lastname: Aas
authors.forename: Alper
authors.initials: A
authors.lastname: Kiraz
authors.forename: Halil
authors.initials: H
authors.lastname: Bayraktar
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D045304:Cytochromes c / Q000737:chemistry*; D031541:Fluorescence Resonance Energy Transfer / Q000379:methods; D006420:Hemeproteins / Q000737:chemistry*; D008164:Luminescent Proteins / Q000737:chemistry*; D010084:Oxidation-Reduction
chemical_list: D001426:Bacterial Proteins; D006420:Hemeproteins; D008164:Luminescent Proteins; C054562:yellow fluorescent protein, Bacteria; D045304:Cytochromes c