-transparent.png){kind=logo}
The coordination of the heme iron in cytochrome c-552 from Euglena gracilis was investigated by 1H NMR studies at 360 MHz. The data imply that the axial heme ligands are His-14 and Met-56 in both the oxidized and the reduced protein. Studies of mixed solutions of ferro- and ferricytochrome c-552, which provided much of the information on the heme structure, also showed that the intermolecular electron exchange is characterized by a bimolecular rate constant of 5-10(6) mol-1-s-1 at 29 degrees C, which is three orders of magnitude faster than the corresponding reaction in solutions of mammalian cytochromes c.
Related Publications
R M Keller, and
K Wüthrich, and
A Schejter
May 1974,
The Biochemical journal,
R M Keller, and
K Wüthrich, and
A Schejter
June 1975,
Archives of biochemistry and biophysics,
R M Keller, and
K Wüthrich, and
A Schejter
December 1988,
Biochemical and biophysical research communications,
R M Keller, and
K Wüthrich, and
A Schejter
May 1977,
Archives of biochemistry and biophysics,
R M Keller, and
K Wüthrich, and
A Schejter
February 1973,
Nature,
R M Keller, and
K Wüthrich, and
A Schejter
May 1963,
Nature,
R M Keller, and
K Wüthrich, and
A Schejter
July 1998,
Biochemistry,
R M Keller, and
K Wüthrich, and
A Schejter
November 1976,
Archives of biochemistry and biophysics,
R M Keller, and
K Wüthrich, and
A Schejter
September 1974,
Archives of biochemistry and biophysics,
R M Keller, and
K Wüthrich, and
A Schejter
September 1998,
Inorganic chemistry,
