ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2008
Submolecular unfolding units of Pseudomonas aeruginosa cytochrome c-551.
Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 17 citations in OpenAlex.
- Cytochrome unfolding pathways from computational analysis of crystal structures.Journal of inorganic biochemistry · 2016Article
- Article
- Redox state dependence of axial ligand dynamics in Nitrosomonas europaea cytochrome c552.The journal of physical chemistry. B · 2013Article
- Methionine ligand lability in bacterial monoheme cytochromes c: an electrochemical study.The journal of physical chemistry. B · 2011Article
- Folding dynamics of phenylalanine hydroxylase depends on the enzyme's metallation state: the native metal, iron, protects against aggregate intermediates.European biophysics journal : EBJ · 2011Article
- Structural and kinetic studies of imidazole binding to two members of the cytochrome c (6) family reveal an important role for a conserved heme pocket residue.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2011Article
- Compressing the free energy range of substructure stabilities in iso-1-cytochrome c.Protein science : a publication of the Protein Society · 2009Article
- The chemistry and biochemistry of heme c: functional bases for covalent attachment.Natural product reports · 2008Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Hydrogen exchange rates for backbone amide protons of oxidized Pseudomonas aeruginosa cytochrome c-551 (P. aeruginosa cytochrome c) have been measured in the presence of low concentrations of the denaturant guanidine hydrochloride. Analysis of the data has allowed identification of submolecular unfolding units known as foldons. The highest-energy foldon bears similarity to the proposed folding intermediate for P. aeruginosa cytochrome c. Parallels are seen to the foldons of the structurally homologous horse cytochrome c, although the heme axial methionine-bearing loop has greater local stability in P. aeruginosa cytochrome c, in accord with previous folding studies. Regions of low local stability are observed to correspond with regions that interact with redox partners, providing a link between foldon properties and function.
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