ArticleInorganic chemistry2010
Variation and analysis of second-sphere interactions and axial histidinate character in c-type cytochromes.
Article in Inorganic chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 31 citations in OpenAlex.
- The two redox states of the human NEET proteins' [2Fe-2S] clusters.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2021Article
- The good, the neutral, and the positive: buffer identity impacts CODalton transactions (Cambridge, England : 2003) · 2019Article
- Structural Origin of the Large Redox-Linked Reorganization in the 2-Oxoglutarate Dependent Oxygenase, TauD.Journal of the American Chemical Society · 2019Article
- 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
- Elucidation of the heme active site electronic structure affecting the unprecedented nitrite dismutase activity of the ferrihemeChemical science · 2016Article
- Modulating the cobalt redox potential through imidazole hydrogen bonding interactions in a supramolecular biomimetic protein-cofactor model.Chemical science · 2016Article
- Design and fine-tuning redox potentials of metalloproteins involved in electron transfer in bioenergetics.Biochimica et biophysica acta · 2016Review
- Effects of protein structure on iron-polypeptide vibrational dynamic coupling in cytochrome c.Biochemistry · 2015Article
- Metalloproteins containing cytochrome, iron-sulfur, or copper redox centers.Chemical reviews · 2014Review
- The role of key residues in structure, function, and stability of cytochrome-c.Cellular and molecular life sciences : CMLS · 2014Review
- The influence of heme ruffling on spin densities in ferricytochromes c probed by heme core 13C NMR.Inorganic chemistry · 2013Article
- 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
- Chemical reactivity of Synechococcus sp. PCC 7002 and Synechocystis sp. PCC 6803 hemoglobins: covalent heme attachment and bishistidine coordination.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2011Article
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2 authors at 1 institution in 1 country.
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Abstract
The electron-donating properties of the axial His ligand to heme iron in cytochromes c (cyts c) are found to be correlated with the midpoint reduction potential (E(m)) in variants of Hydrogenobacter thermophilus cytochrome c(552) (Ht cyt c(552)) in which mutations have been made in and near the Cys-X-X-Cys-His (CXXCH) heme-binding motif. To probe the strength of the His-Fe(III) interaction, we have measured (13)C nuclear magnetic resonance (NMR) chemical shifts for (13)CN(-) bound to heme iron trans to the axial His in Ht Fe(III) cyt c(552) variants. We observe a linear relationship between these (13)C chemical shifts and E(m), indicating that the His-Fe(III) bond strength correlates with E(m). To probe a conserved hydrogen bonding interaction between the axial His Hdelta1 and the backbone carbonyl of a Pro residue, we measured the pK(a) of the axial His Hdelta1 proton (pK(a(2))), which we propose to relate to the His-Fe(III) interaction, reduction potential, and local electrostatic effects. The observed linear relationship between the axial His (13)Cbeta chemical shift and E(m) is proposed to reflect histidinate (anionic) character of the ligand. A linear relationship also is seen between the average heme methyl (1)H chemical shift and E(m) which may reflect variation in axial His electron-donating properties or in the ruffling distortion of the heme plane. In summary, chemical shifts of the axial His and exogenous CN(-) bound trans to His are shown to be sensitive probes of the His-Fe(III) interaction in variants of Ht cyt c(552) and display trends that correlate with E(m).
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