Literature DB >> 6244160

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

G R Moore, R J Williams.   

Abstract

The pH dependence and the temperature dependence of the nuclear magnetic resonance spectrum of horse ferrocytochrome c are described. This protein is very stable; it maintains an ordered structure over the pH range 4 to 12 at 25 degrees C and over the temperature range 4 degrees C to 97 degrees C at pH 7.0. The dynamic characteristics of the conformation of ferrocytochrome c were investigated. Particular emphasis was laid on the aromatic resonances and resonances of methyl groups shifted far upfield. Tyr-48 and Phe-46 were found to be relatively immobile whilst a region of the protein close to Ile-57 was found to be relatively flexible.

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Year:  1980        PMID： 6244160     DOI： 10.1111/j.1432-1033.1980.tb05975.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN： 0014-2956


  9 in total

1.  Structure-function relationship of reduced cytochrome c probed by complete solution structure determination in 30% acetonitrile/water solution.

Authors:  Sivashankar G Sivakolundu; Patricia Ann Mabrouk
Journal:  J Biol Inorg Chem       Date:  2003-02-15       Impact factor: 3.358

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

Authors:  R T Hartshorn; G R Moore
Journal:  Biochem J       Date:  1989-03-01       Impact factor: 3.857

3.  Proton hyperfine resonance assignments using the nuclear Overhauser effect for ferric forms of horse and tuna cytochrome c.

Authors:  J D Satterlee; S Moench
Journal:  Biophys J       Date:  1987-07       Impact factor: 4.033

4.  Near-exact enthalpy-entropy compensation governs the thermal unfolding of protonation states of oxidized cytochrome c.

Authors:  Jonathan B Soffer; Reinhard Schweitzer-Stenner
Journal:  J Biol Inorg Chem       Date:  2014-07-17       Impact factor: 3.358

Review 5.  Relating the multi-functionality of cytochrome c to membrane binding and structural conversion.

Authors:  Reinhard Schweitzer-Stenner
Journal:  Biophys Rev       Date:  2018-03-24

6.  Metalloprotein entatic control of ligand-metal bonds quantified by ultrafast x-ray spectroscopy.

Authors:  Michael W Mara; Ryan G Hadt; Marco Eli Reinhard; Thomas Kroll; Hyeongtaek Lim; Robert W Hartsock; Roberto Alonso-Mori; Matthieu Chollet; James M Glownia; Silke Nelson; Dimosthenis Sokaras; Kristjan Kunnus; Keith O Hodgson; Britt Hedman; Uwe Bergmann; Kelly J Gaffney; Edward I Solomon
Journal:  Science       Date:  2017-06-23       Impact factor: 47.728

7.  Structural role of the tyrosine residues of cytochrome c.

Authors:  C G Eley; G R Moore; R J Williams; W Neupert; P J Boon; H H Brinkhof; R J Nivard; G I Tesser
Journal:  Biochem J       Date:  1982-07-01       Impact factor: 3.857

8.  The conformation of eukaryotic cytochrome c around residues 39, 57, 59 and 74.

Authors:  M N Robinson; A P Boswell; Z X Huang; C G Eley; G R Moore
Journal:  Biochem J       Date:  1983-09-01       Impact factor: 3.857

9.  Ionization of tyrosine and lysine residues in native and modified horse cytochrome c.

Authors:  A P Boswell; G R Moore; R J Williams; D E Harris; C J Wallace; S Bocieck; D Welti
Journal:  Biochem J       Date:  1983-09-01       Impact factor: 3.857
  9 in total

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