Journal article
Design of a Ruthenium-Labeled Cytochrome c Derivative to Study Electron Transfer with the Cytochrome bc 1 Complex
Biochemistry (Easton), v 42(10), pp 2816-2824
18 Mar 2003
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Abstract
A new ruthenium-cytochrome c derivative was designed to study electron transfer from cytochrome bc1 to cytochrome c (Cc). The single sulfhydryl on yeast H39C;C102T iso-1-Cc was labeled with Ru(2,2‘-bipyrazine)2(4-bromomethyl-4‘-methyl-2,2‘-bipyridine) to form Ruz-39-Cc. The Ruz-39-Cc derivative has the same steady-state activity with yeast cytochrome bc1 as wild-type yeast iso-1-Cc, indicating that the ruthenium complex does not interfere in the binding interaction. Laser excitation of reduced Ruz-39-Cc results in electron transfer from heme c to the excited state of ruthenium with a rate constant of 1.5 × 106 s-1. The resulting Ru(I) is rapidly oxidized by atmospheric oxygen in the buffer. The yield of photooxidized heme c is 20% in a single flash. Flash photolysis of a 1:1 complex between reduced yeast cytochrome bc1 and Ruz-39-Cc at low ionic strength leads to rapid photooxidation of heme c, followed by intracomplex electron transfer from cytochrome c1 to heme c with a rate constant of 1.4 × 104 s-1. As the ionic strength is raised above 100 mM, the intracomplex phase disappears, and a new phase appears due to the bimolecular reaction between solution Ru-39-Cc and cytochrome bc1. The interaction of yeast Ru-39-Cc with yeast cytochrome bc1 is stronger than that of horse Ru-39-Cc with bovine cytochrome bc1, suggesting that nonpolar interactions are stronger in the yeast system.
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Details
- Title
- Design of a Ruthenium-Labeled Cytochrome c Derivative to Study Electron Transfer with the Cytochrome bc 1 Complex
- Creators
- Gregory Engstrom - University of Arkansas at FayettevilleRay Rajagukguk - University of Arkansas at FayettevilleAleister J. Saunders - University of Arkansas at FayettevilleChetan N. Patel - Oklahoma State UniversitySany Rajagukguk - University of Arkansas at FayettevilleTorsten Merbitz-Zahradnik - University of Arkansas at FayettevilleKunhong Xiao - University of Arkansas at FayettevilleGary J. Pielak - University of Arkansas at FayettevilleBernard Trumpower - University of Arkansas at FayettevilleChang-An Yu - University of Arkansas at FayettevilleLinda Yu - University of Arkansas at FayettevilleBill Durham - University of Arkansas at FayettevilleFrancis Millett - University of Arkansas at Fayetteville
- Publication Details
- Biochemistry (Easton), v 42(10), pp 2816-2824
- Publisher
- American Chemical Society; Washington, DC
- Number of pages
- 9
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Biology
- Web of Science ID
- WOS:000181535300008
- Scopus ID
- 2-s2.0-0037452991
- Other Identifier
- 991021448188704721
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- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Biochemistry & Molecular Biology