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• W2120577964 startingPage "1361" @default.
• W2120577964 abstract "In Escherichia coli cytochrome c maturation requires a set of eight proteins including the heme chaperone CcmE, which binds heme transiently, yet covalently. Several variants of CcmE were purified and analyzed by continuous-wave electron paramagnetic resonance, electron nuclear double resonance, and hyperfine sublevel correlation spectroscopy to investigate the heme axial coordination. Results reveal the presence of a number of coordination environments, two high-spin heme centers with different rhombicities, and at least one low-spin heme center. The low-spin species was shown to be an artifact induced by the presence of available histidines in the vicinity of the iron. Both of the high-spin forms are five-coordinated, and comparison of the spectra of the wild-type CcmE with those of the mutant CcmEY134H proves that the higher-rhombicity form is coordinated by Tyr134. The low-rhombicity (axial) form does not have a histidine residue or a water molecule as an axial ligand. However, we identified exchangeable protons coupled to the iron ion. We propose that the axial form can be coordinated by a carboxyl group of an acidic residue in the flexible domain of the protein. The two species would represent two different conformations of the flexible α-helix domain surrounding the heme. This conformational flexibility confers CcmE special dynamic properties that are certainly important for its function." @default.
• W2120577964 created "2016-06-24" @default.
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• W2120577964 date "2007-02-01" @default.
• W2120577964 modified "2023-09-30" @default.
• W2120577964 title "Axial Coordination of Heme in Ferric CcmE Chaperone Characterized by EPR Spectroscopy" @default.
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• W2120577964 doi "https://doi.org/10.1529/biophysj.106.098277" @default.
• W2120577964 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1783872" @default.
• W2120577964 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/17142277" @default.
• W2120577964 hasPublicationYear "2007" @default.
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