ArticleProceedings of the National Academy of Sciences of the United States of America2004
Heme axial methionine fluxionality in Hydrogenobacter thermophilus cytochrome c552.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 49 citations in OpenAlex.
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- Towards Bacterial Resistance via the Membrane Strategy: Enzymatic, Biophysical and Biomimetic Studies of the Lipid cis-trans Isomerase of Pseudomonas aeruginosa.Chembiochem : a European journal of chemical biology · 2025Article
- Heme-Protein Interactions and Functional Relevant Heme Deformations: The Cytochrome c Case.Molecules (Basel, Switzerland) · 2022Review
- Unusual CytochromeInternational journal of molecular sciences · 2022Article
- Structural basis for heme detoxification by an ATP-binding cassette-type efflux pump in gram-positive pathogenic bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Contributions to cytochromeChemical science · 2021Article
- Solution of a Puzzle: High-Level Quantum-Chemical Treatment of Pseudocontact Chemical Shifts Confirms Classic Semiempirical Theory.The journal of physical chemistry letters · 2020Article
- Influence of heme c attachment on heme conformation and potential.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Article
- NMR investigations of nitrophorin 2 belt side chain effects on heme orientation and seating of native N-terminus NP2 and NP2(D1A).Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014Article
- Overexpression, purification, and enthalpy of unfolding of ferricytochrome c552 from a psychrophilic microorganism.Journal of inorganic biochemistry · 2014Article
- Redox state dependence of axial ligand dynamics in Nitrosomonas europaea cytochrome c552.The journal of physical chemistry. B · 2013Article
- The influence of heme ruffling on spin densities in ferricytochromes c probed by heme core 13C NMR.Inorganic chemistry · 2013Article
- Structural characterization of nitrosomonas europaea cytochrome c-552 variants with marked differences in electronic structure.Chembiochem : a European journal of chemical biology · 2013Article
- Heme-protein vibrational couplings in cytochrome c provide a dynamic link that connects the heme-iron and the protein surface.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Modulation of ligand-field parameters by heme ruffling in cytochromes c revealed by EPR spectroscopy.Inorganic chemistry · 2011Article
- Methionine ligand lability in bacterial monoheme cytochromes c: an electrochemical study.The journal of physical chemistry. B · 2011Article
- Comparing substrate specificity between cytochrome c maturation and cytochrome c heme lyase systems for cytochrome c biogenesis.Metallomics : integrated biometal science · 2011Article
- Variation and analysis of second-sphere interactions and axial histidinate character in c-type cytochromes.Inorganic chemistry · 2010Article
- NMR and DFT investigation of heme ruffling: functional implications for cytochrome c.Journal of the American Chemical Society · 2010Article
- Heme-coordinating inhibitors of neuronal nitric oxide synthase. Iron-thioether coordination is stabilized by hydrophobic contacts without increased inhibitor potency.Journal of the American Chemical Society · 2010Article
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6 authors at 1 institution in 1 country.
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Abstract
The heme group in paramagnetic (S = 1/2) ferricytochromes c typically displays a markedly asymmetric distribution of unpaired electron spin density among the heme pyrrole beta substituents. This asymmetry is determined by the orientations of the heme axial ligands, histidine and methionine. One exception to this is ferricytochrome c(552) from Hydrogenobacter thermophilus, which has similar amounts of unpaired electron spin density at the beta substituents on all four heme pyrroles. Here, determination of the orientation of the magnetic axes and analysis of NMR line shapes for H. thermophilus ferricytochrome c(552) is performed. These data reveal that the unusual electronic structure for this protein is a result of fluxionality of the heme axial methionine. It is proposed that the ligand undergoes inversion at the pyramidal sulfur, and the rapid interconversion between two diastereomeric forms results in the unusual heme electronic structure. Thus a fluxional process for a metal-bound amino acid side chain has now been identified.
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