Literature DB >> 6257839

Nuclear magnetic resonance studies of the phenylalanine residues of eukaryotic cytochrome c.

A P Boswell, G R Moore, R J Williams, J C Chien, L C Dickinson.   

Abstract

The resonances of Phe 82 and Phe 10 in the nuclear magnetic resonance spectra of horse cytochrome c are reassigned using nuclear Overhauser enhancements. The reassignments provide new information about the oxidation state linked conformation change of cytochrome c. The region of the protein now known to be affected by the change extends to the part of the protein close to Phe 10.

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Year:  1980        PMID： 6257839     DOI： 10.1016/s0162-0134(00)80254-8

Source DB:  PubMed          Journal:  J Inorg Biochem        ISSN： 0162-0134            Impact factor:   4.155


  4 in total

1.  Chemical exchange in two dimensions in the 1H NMR assignment of cytochrome c.

Authors:  Y Q Feng; A J Wand; H Roder; S W Englander
Journal:  Biophys J       Date:  1991-02       Impact factor: 4.033

2.  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

3.  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

4.  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
  4 in total

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