ArticleInorganic chemistry2018
Ligation and Reactivity of Methionine-Oxidized Cytochrome c.
Article in Inorganic chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- Disabling the Entatic Control of Methionine Ligation through Additive Destabilization of Ferric CytochromeInorganic chemistry · 2025Article
- Synthesis and Biological Activities of Some Metal Complexes of Peptides: A Review.Biotech (Basel (Switzerland)) · 2024Review
- Spectroelectrochemistry for determination of the redox potential in heme enzymes: Dye-decolorizing peroxidases.BBA advances · 2024Article
- Resonance Raman Studies on Heme Ligand Stretching Modes in Methionine80-Depleted CytochromeThe journal of physical chemistry. B · 2023Article
- Studying Peptide-Metal Ion Complex Structures by Solution-State NMR.International journal of molecular sciences · 2022Review
- Wheel and Deal in the Mitochondrial Inner Membranes: The Tale of CytochromeOxidative medicine and cellular longevity · 2020Review
- 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
- Lysine carbonylation is a previously unrecognized contributor to peroxidase activation of cytochromeChemical science · 2019Article
- The K79G Mutation Reshapes the Heme Crevice and Alters Redox Properties of Cytochrome c.Biochemistry · 2018Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Met80, one of the heme iron ligands in cytochrome c (cyt c), is readily oxidized to Met sulfoxide (Met-SO) by several biologically relevant oxidants. The modification has been suggested to affect both the electron-transfer (ET) and apoptotic functions of this metalloprotein. The coordination of the heme iron in Met-oxidized cyt c (Met-SO cyt c) is critical for both of these functions but has remained poorly defined. We present electronic absorption, NMR, and EPR spectroscopic investigations as well as kinetic studies and mutational analyses to identify the heme iron ligands in yeast iso-1 Met-SO cyt c. Similar to the alkaline form of native cyt c, Lys73 and Lys79 ligate to the ferric heme iron in the Met80-oxidized protein, but this coordination takes place at much lower pH. The ferrous heme iron is ligated by Met-SO, implying the redox-linked ligand switch in the modified protein. Binding studies with the model peptide microperoxidase-8 provide a rationale for alterations in ligation and for the role of the polypeptide packing in native and Met-SO cyt c. Imidazole binding experiments have revealed that Lys dissociation from the ferric heme in K73A/K79G/M80K (M80K
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.