ArticleProceedings of the National Academy of Sciences of the United States of America2014
Redox-dependent stability, protonation, and reactivity of cysteine-bound heme proteins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- Differences in functional cross-talk between loops C and D in two mitochondrial cytochromes.Journal of inorganic biochemistry · 2026Article
- Methionine coordination to the heme iron and its displacement by nitric oxide in the CcoP subunit of Pseudomonas aeruginosa cytochrome cbbJournal of inorganic biochemistry · 2026Article
- Disabling the Entatic Control of Methionine Ligation through Additive Destabilization of Ferric CytochromeInorganic chemistry · 2025Article
- Gas Tunnel Engineering of Prolyl Hydroxylase Reprograms Hypoxia Signaling in Cells.Angewandte Chemie (International ed. in English) · 2024Article
- ConservedBiochemistry · 2024Article
- Gas tunnel engineering of prolyl hydroxylase reprograms hypoxia signaling in cells.bioRxiv : the preprint server for biology · 2024Article
- Pathogenic Homocystinuria-Associated T236N Mutation Dramatically Alters the Biochemical Properties of Cystathionine Beta-Synthase Protein.Biomedicines · 2024Article
- Crystal Structure and Biochemical Analysis of a Cytochrome P450 Steroid Hydroxylase (Journal of microbiology and biotechnology · 2023Article
- Influence of the Interdomain Interface on Structural and Redox Properties of Multiheme Proteins.Inorganic chemistry · 2022Article
- Reaction of Thiosulfate Dehydrogenase with a Substrate Mimic Induces Dissociation of the Cysteine Heme Ligand Giving Insights into the Mechanism of Oxidative Catalysis.Journal of the American Chemical Society · 2022Article
- A novel catalytic heme cofactor in SfmD with a single thioether bond and aChemical science · 2021Article
- Discovery of a functional, contracted heme-binding motif within a multiheme cytochrome.The Journal of biological chemistry · 2019Article
- A Heme Propionate Staples the Structure of CytochromeInorganic chemistry · 2019Article
- The heme-sensitive regulator SbnI has a bifunctional role in staphyloferrin B production byThe Journal of biological chemistry · 2019Article
- The K79G Mutation Reshapes the Heme Crevice and Alters Redox Properties of Cytochrome c.Biochemistry · 2018Article
- Ligation and Reactivity of Methionine-Oxidized Cytochrome c.Inorganic chemistry · 2018Article
- Totally synthetic microperoxidase-11.Royal Society open science · 2018Article
- Structure and Catalysis of Fe(III) and Cu(II) Microperoxidase-11 Interacting with the Positively Charged Interfaces of Lipids.Molecules (Basel, Switzerland) · 2017Article
- Potentiation of hydrogen peroxide toxicity: From catalase inhibition to stable DNA-iron complexes.Mutation research. Reviews in mutation research · 2017Review
- Remote Perturbations in Tertiary Contacts Trigger Ligation of Lysine to the Heme Iron in Cytochrome c.Biochemistry · 2017Article
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5 authors.
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Abstract
Cysteine-bound hemes are key components of many enzymes and biological sensors. Protonation (deprotonation) of the Cys ligand often accompanies redox transformations of these centers. To characterize these phenomena, we have engineered a series of Thr78Cys/Lys79Gly/Met80X mutants of yeast cytochrome c (cyt c) in which Cys78 becomes one of the axial ligands to the heme. At neutral pH, the protonation state of the coordinated Cys differs for the ferric and ferrous heme species, with Cys binding as a thiolate and a thiol, respectively. Analysis of redox-dependent stability and alkaline transitions of these model proteins, as well as comparisons to Cys binding studies with the minimalist heme peptide microperoxidase-8, demonstrate that the protein scaffold and solvent interactions play important roles in stabilizing a particular Cys-heme coordination. The increased stability of ferric thiolate compared with ferrous thiol arises mainly from entropic factors. This robust cyt c model system provides access to all four forms of Cys-bound heme, including the ferric thiol. Protein motions control the rates of heme redox reactions, and these effects are amplified at low pH, where the proteins are less stable. Thermodynamic signatures and redox reactivity of the model Cys-bound hemes highlight the critical role of the protein scaffold and its dynamics in modulating redox-linked transitions between thiols and thiolates.
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