Literature DB >> 2539812

A denaturation-induced proton-uptake study of horse ferricytochrome c.

R T Hartshorn1, G R Moore.   

Abstract

The observation that 6 M-urea denatures horse ferricytochrome c in the pH range 4-6, but not horse ferrocytochrome c, has been exploited to determine the denaturation-induced proton uptake of ferricytochrome c. This is related to the pKa values of ionizable groups buried within the native protein. The data indicate that one of the haem propionic acid substituents of ferricytochrome c has a pKa of less than 4.5, whereas the other has a pKa of greater than 9.

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Year:  1989        PMID： 2539812      PMCID： PMC1138402          DOI： 10.1042/bj2580595

Source DB:  PubMed          Journal:  Biochem J        ISSN： 0264-6021            Impact factor:   3.857


  17 in total

1.  Horse heart cytochrome c. The oxidation-reduction potential and protein structures.

Authors:  Y P Myer; A F Saturno; B C Verma; A Pande
Journal:  J Biol Chem       Date:  1979-11-25       Impact factor: 5.157

2.  The crystal structure of bonito (katsuo) ferrocytochrome c at 2.3 A resolution. II. Structure and function.

Authors:  N Tanaka; T Yamane; T Tsukihara; T Ashida; M Kakudo
Journal:  J Biochem       Date:  1975-01-01       Impact factor: 3.387

3.  Hydrogen ion titration of horse heart ferricytochrome c.

Authors:  R W Shaw; C R Hartzell
Journal:  Biochemistry       Date:  1976-05-04       Impact factor: 3.162

4.  Spectroscopic studies on the conformation of cytochrome c and apocytochrome c.

Authors:  J S Cohen; W R Fisher; A N Schechter
Journal:  J Biol Chem       Date:  1974-02-25       Impact factor: 5.157

5.  The Trp-59 fluorescence of ferricytochrome c as a sensitive measure of the over-all protein conformation.

Authors:  T Y Tsong
Journal:  J Biol Chem       Date:  1974-03-25       Impact factor: 5.157

6.  Some aspects of pH and temperature dependence of the NMR spectra of cytochrome C.

Authors:  R K Gupta; S H Koenig
Journal:  Biochem Biophys Res Commun       Date:  1971-12-03       Impact factor: 3.575

7.  Analysis of the ionization constants and heats of ionization of reduced and oxidized horse heart cytochrome c.

Authors:  M A Marini; C J Martin; R L Berger; L Forlani
Journal:  Biopolymers       Date:  1981-10       Impact factor: 2.505

8.  Nuclear-magnetic-resonance studies of ferrocytochrome c. pH and temperature dependence.

Authors:  G R Moore; R J Williams
Journal:  Eur J Biochem       Date:  1980-02

9.  The conformation of cytochrome c in solution. Localization of a conformational difference between ferri- and ferrocytochrome c on the surface of the molecule.

Authors:  H R Bosshard; M Zürrer
Journal:  J Biol Chem       Date:  1980-07-25       Impact factor: 5.157

10.  Fourier-transform infra-red studies of the alkaline isomerization of mitochondrial cytochrome c and the ionization of carboxylic acids.

Authors:  P Tonge; G R Moore; C W Wharton
Journal:  Biochem J       Date:  1989-03-01       Impact factor: 3.857
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  10 in total

1.  Resolving the individual components of a pH-induced conformational change.

Authors:  C Blouin; J G Guillemette; C J Wallace
Journal:  Biophys J       Date:  2001-10       Impact factor: 4.033

2.  Selective excitation of native fluctuations during thermal unfolding simulations: horse heart cytochrome c as a case study.

Authors:  Danilo Roccatano; Isabella Daidone; Marc-Antoine Ceruso; Cecilia Bossa; Alfredo Di Nola
Journal:  Biophys J       Date:  2003-03       Impact factor: 4.033

3.  Naturally Occurring A51V Variant of Human Cytochrome c Destabilizes the Native State and Enhances Peroxidase Activity.

Authors:  Haotian Lei; Bruce E Bowler
Journal:  J Phys Chem B       Date:  2019-10-14       Impact factor: 2.991

4.  Remote Perturbations in Tertiary Contacts Trigger Ligation of Lysine to the Heme Iron in Cytochrome c.

Authors:  Jie Gu; Dong-Woo Shin; Ekaterina V Pletneva
Journal:  Biochemistry       Date:  2017-05-31       Impact factor: 3.162

5.  The heme redox center of chloroplast cytochrome f is linked to a buried five-water chain.

Authors:  S E Martinez; D Huang; M Ponomarev; W A Cramer; J L Smith
Journal:  Protein Sci       Date:  1996-06       Impact factor: 6.725

6.  A Compact Structure of Cytochrome c Trapped in a Lysine-Ligated State: Loop Refolding and Functional Implications of a Conformational Switch.

Authors:  Jeanine F Amacher; Fangfang Zhong; George P Lisi; Michael Q Zhu; Stephanie L Alden; Kevin R Hoke; Dean R Madden; Ekaterina V Pletneva
Journal:  J Am Chem Soc       Date:  2015-06-24       Impact factor: 15.419

7.  Histidine-Lysine Axial Ligand Switching in a Hemoglobin: A Role for Heme Propionates.

Authors:  Dillon B Nye; Matthew R Preimesberger; Ananya Majumdar; Juliette T J Lecomte
Journal:  Biochemistry       Date:  2018-01-10       Impact factor: 3.162

8.  The response of Ω-loop D dynamics to truncation of trimethyllysine 72 of yeast iso-1-cytochrome c depends on the nature of loop deformation.

Authors:  Levi J McClelland; Sean M Seagraves; Md Khurshid Alam Khan; Melisa M Cherney; Swati Bandi; Justin E Culbertson; Bruce E Bowler
Journal:  J Biol Inorg Chem       Date:  2015-05-07       Impact factor: 3.358

9.  Fourier-transform infra-red studies of the alkaline isomerization of mitochondrial cytochrome c and the ionization of carboxylic acids.

Authors:  P Tonge; G R Moore; C W Wharton
Journal:  Biochem J       Date:  1989-03-01       Impact factor: 3.857

10.  The K79G Mutation Reshapes the Heme Crevice and Alters Redox Properties of Cytochrome c.

Authors:  Yunling Deng; Fangfang Zhong; Stephanie L Alden; Kevin R Hoke; Ekaterina V Pletneva
Journal:  Biochemistry       Date:  2018-09-24       Impact factor: 3.162
  10 in total

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