Preparation and characterization of a pentaammineruthenium(III) derivative of horse heart ferricytochrome c.

Abstract:

:A stable complex between pentaammineruthenium(III) and histidine-33 in horse heart ferricytochrome c is formed in the reaction between aquopentaammineruthenium(II) and the protein at pH 7. HPLC of the tryptic hydrolysate of the modified protein was employed to identify the pentaammineruthenium binding site. Spectroscopic measurements show that the integrity of the native structure in the vicinity of the heme c group is maintained in the ruthenium-modified protein. The reduction potentials are: heme c (Fe3+/2+), 0.26 V; Ru(NH3)5(His-33)3+/2+, 0.15 V (vs. normal hydrogen electrode).

authors

Yocom KM,Shelton JB,Shelton JR,Schroeder WA,Worosila G,Isied SS,Bordignon E,Gray HB

doi

10.1073/pnas.79.22.7052

subject

Has Abstract

pub_date

1982-11-01 00:00:00

pages

7052-5

issue

22

eissn

0027-8424

issn

1091-6490

journal_volume

79

pub_type

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