A model for the misfolded bis-His intermediate of cytochrome c: the 1-56 N-fragment.

No abstract is available for this paper.

• Publication year

  2004

• Venue

  Journal of Inorganic Biochemistry

• Publication date

  2004-06-01

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1016/J.JINORGBIO.2004.02.026PMID 15149817
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Denaturant dependence of equilibrium unfolding intermediates and denatured state structure of horse ferricytochrome c

  2002cited by this paper
• Kinetic barriers to the folding of horse cytochrome C in the reduced state.

  2002cited by this paper
• Spectroscopic Characterization of Nonnative Conformational States of Cytochrome c

  2002cited by this paper
• Cytochrome c reconstituted from two peptide fragments displays native-like redox properties.

  2001cited by this paper
• Effect of pH on axial ligand coordination of cytochrome c" from Methylophilus methylotrophus and horse heart cytochrome c.

  2000cited by this paper
• The heme-containing N-fragment (residues 1-56) of cytochrome c is a bis-histidine functional system.

  2000cited by this paper
• X-ray Crystal Structure and Characterization of Halide-binding Sites of Human Myeloperoxidase at 1.8 Å Resolution*

  2000cited by this paper
• Characterization of equilibrium intermediates in denaturant-induced unfolding of ferrous and ferric cytochromes c using magnetic circular dichroism, circular dichroism, and optical absorption spectroscopies.

  2000cited by this paper
• The Role of the Distal and Proximal Protein Environments in Controlling the Ferric Spin State and in Stabilizing Thiolate Ligation in Heme Systems: Thiolate Adducts of the Myoglobin H93G Cavity Mutant

  1999cited by this paper
• Structural organization in peptide fragments of cytochrome c by heme binding.

  1999cited by this paper
• Pentacoordinate hemin derivatives in sodium dodecyl sulfate micelles: model systems for the assignment of the fifth ligand in ferric heme proteins.

  1999cited by this paper
• Ligand Exchange during Unfolding of Cytochrome c *

  1999cited by this paper
• Cytochrome c Folding and Unfolding: A Biphasic Mechanism

  1998cited by this paper
• Folding intermediates in cytochrome c

  1998cited by this paper
• Understanding heme cavity structure of peroxidases: comparison of electronic absorption and resonance Raman spectra with crystallographic results.

  1998cited by this paper
• Submillisecond protein folding kinetics studied by ultrarapid mixing.

  1997cited by this paper
• Folding of cytochrome c initiated by submillisecond mixing

  1997cited by this paper
• Ligand exchange during cytochrome c folding

  1997cited by this paper
• Identification of the predominant non-native histidine ligand in unfolded cytochrome c.

  1997cited by this paper
• Role of heme axial ligands in the conformational stability of the native and molten globule states of horse cytochrome c.

  1996cited by this paper
• Direct electrochemical evidence for an equilibrium intermediate in the guanidine-induced unfolding of cytochrome c.

  1996cited by this paper
• Secondary and tertiary structure of the A‐state of cytochrome c from resonance Raman spectroscopy

  1995cited by this paper
• Limited proteolysis of cytochrome c in trifluoroethanol

  1995cited by this paper
• Correlations between Raman frequencies and structure for planar and nonplanar metalloporphyrins

  1994cited by this paper
• Time-resolved absorption and magnetic circular dichroism spectroscopy of cytochrome c3 from Desulfovibrio.

  1993cited by this paper
• Complete assignment of cytochrome c resonance Raman spectra via enzymic reconstitution with isotopically labeled hemes

  1993cited by this paper
• Oxidation state-dependent conformational changes in cytochrome c.

  1992cited by this paper
• Mechanism of acid-induced folding of proteins.

  1990cited by this paper
• Unfolding and flexibility in hemoproteins shown in the case of carboxymethylated cytochrome c.

  1987cited by this paper
• Biological applications of Raman spectroscopy

  1987cited by this paper
• Structural correlations and vinyl influences in resonance Raman spectra of protoheme complexes and proteins

  1982cited by this paper
• Resonance Raman spectroscopy of heme proteins with intensified vidicon detectors: Studies of low frequency modes and excitation profiles in cytochrome c and hemoglobin

  1980cited by this paper
• A biologically active, three-fragment complex of horse heart cytochrome c.

  1980cited by this paper
• Urea denaturation of horse heart ferricytochrome c. Equilibrium studies and characterization of intermediate forms.

  1980cited by this paper
• Hydrogen-bond and deprotonation effects on the resonance Raman iron-imidazole mode in deoxyhemoglobin models: implications for hemoglobin cooperativity

  1980cited by this paper
• Resonance Raman spectra of metallooctaethylporphyrins. Structural probe of metal displacement

  1975cited by this paper
• Reconstitution of horse heart cytochrome c: reformation of the peptide bond linking residues 65 and 66.

  1974cited by this paper
• SOME ASPECTS OF METALLOPORPHYRIN STEREOCHEMISTRY *

  1973cited by this paper
• Reconstitution of horse heart cytochrome c: interaction of the components obtained upon cleavage of the peptide bond following methionine residue 65.

  1971cited by this paper

• Correlated electric field modulation of electron transfer parameters and the access to alternative conformations of multifunctional cytochrome c.

  2021cites this paper
• Cytochrome c: An extreme multifunctional protein with a key role in cell fate.

  2019cites this paper
• Refolding kinetics of cytochrome c studied with microsecond timescale continuous-flow UV-vis spectroscopy and rapid freeze-quench EPR.

  2018cites this paper
• Probing the non‐native states of Cytochrome c with resonance Raman spectroscopy: A tool for investigating the structure–function relationship

  2018cites this paper
• Surface Engineering of Gold Nanorods for Cytochrome c Bioconjugation: An Effective Strategy To Preserve the Protein Structure

  2018cites this paper
• Engineered holocytochrome c synthases that biosynthesize new cytochromes c

  2017cites this paper
• Unravelling the Non-Native Low-Spin State of the Cytochrome c-Cardiolipin Complex: Evidence of the Formation of a His-Ligated Species Only.

  2017cites this paper
• The Met80Ala and Tyr67His/Met80Ala mutants of human cytochrome c shed light on the reciprocal role of Met80 and Tyr67 in regulating ligand access into the heme pocket.

  2017cites this paper
• Structural changes and picosecond to second dynamics of cytochrome c in interaction with nitric oxide in ferrous and ferric redox states.

  2017cites this paper
• Multifunctional Cytochrome c: Learning New Tricks from an Old Dog.

  2017cites this paper
• Structure-function relationships in human cytochrome c: The role of tyrosine 67.

  2016cites this paper
• Active Site Structure and Peroxidase Activity of Oxidatively Modified Cytochrome c Species in Complexes with Cardiolipin.

  2015cites this paper
• Immobilized cytochrome c bound to cardiolipin exhibits peculiar oxidation state-dependent axial heme ligation and catalytically reduces dioxygen

  2015cites this paper
• Role of lysines in cytochrome c-cardiolipin interaction.

  2013cites this paper
• Extended cardiolipin anchorage to cytochrome c: a model for protein–mitochondrial membrane binding

  2010cites this paper
• Resonance Raman studies of the (His)(Cys)3 2Fe-2S cluster of MitoNEET: comparison to the (Cys)4 mutant and implications of the effects of pH on the labile metal center.

  2009influential citation
• A novel DNA biosensor based on ssDNA/Cyt c/l-Cys/GNPs/Chits/GCE

  2009cites this paper
• Optical manipulation of proteins in aqueous solution

  2009cites this paper
• Electrochemical studies of cytochrome c on gold electrodes with promotor of humic acid and 4-aminothiophenol

  2007influential citation
• Heme coordination states of unfolded ferrous cytochrome C.

  2006cites this paper
• Ultrafast heme dynamics in ferrous versus ferric cytochrome c studied by time-resolved resonance Raman and transient absorption spectroscopy.

  2006cites this paper
• Insights into the role of the histidines in the structure and stability of cytochrome c

  2005cites this paper
• Heme binding by the N-terminal fragment 1-44 of human growth hormone.

  2005cites this paper
• Effect of sol–gel encapsulation on the unfolding of ferric horse heart cytochrome c

  2005cites this paper
• Protein Unfolding: 1H‐NMR Studies of Paramagnetic Ferricytochrome c‐550 from Horse Heart

  2005cites this paper
• ATP specifically drives refolding of non‐native conformations of cytochrome c

  2005cites this paper
• Kinetics of Histidine Dissociation From the Heme Fe(III) in N-fragment (residues 1–56) of Cytochrome c

  2004cites this paper
• Photodissociation of heme distal methionine in ferrous cytochrome C revealed by subpicosecond time-resolved resonance Raman spectroscopy.

  2004cites this paper
• The 40s Ω-loop plays a critical role in the stability and the alkaline conformational transition of cytochrome c

  2004cites this paper