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Design of a ruthenium-labeled cytochrome c derivative to study electron transfer with the cytochrome bc1 complex.

Publication ,  Journal Article
Engstrom, G; Rajagukguk, R; Saunders, AJ; Patel, CN; Rajagukguk, S; Merbitz-Zahradnik, T; Xiao, K; Pielak, GJ; Trumpower, B; Yu, C-A; Yu, L ...
Published in: Biochemistry
March 18, 2003

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 Ru(z)-39-Cc. The Ru(z)-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 Ru(z)-39-Cc results in electron transfer from heme c to the excited state of ruthenium with a rate constant of 1.5 x 10(6) x 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 Ru(z)-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 x 10(4) x 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.

Duke Scholars

Published In

Biochemistry

DOI

ISSN

0006-2960

Publication Date

March 18, 2003

Volume

42

Issue

10

Start / End Page

2816 / 2824

Location

United States

Related Subject Headings

  • Saccharomyces cerevisiae Proteins
  • Ruthenium
  • Photolysis
  • Osmolar Concentration
  • Organometallic Compounds
  • Models, Chemical
  • Kinetics
  • Heme
  • Electron Transport Complex III
  • Electron Transport
 

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Engstrom, G., Rajagukguk, R., Saunders, A. J., Patel, C. N., Rajagukguk, S., Merbitz-Zahradnik, T., … Millett, F. (2003). Design of a ruthenium-labeled cytochrome c derivative to study electron transfer with the cytochrome bc1 complex. Biochemistry, 42(10), 2816–2824. https://doi.org/10.1021/bi027213g
Engstrom, Gregory, Ray Rajagukguk, Aleister J. Saunders, Chetan N. Patel, Sany Rajagukguk, Torsten Merbitz-Zahradnik, Kunhong Xiao, et al. “Design of a ruthenium-labeled cytochrome c derivative to study electron transfer with the cytochrome bc1 complex.Biochemistry 42, no. 10 (March 18, 2003): 2816–24. https://doi.org/10.1021/bi027213g.
Engstrom G, Rajagukguk R, Saunders AJ, Patel CN, Rajagukguk S, Merbitz-Zahradnik T, et al. Design of a ruthenium-labeled cytochrome c derivative to study electron transfer with the cytochrome bc1 complex. Biochemistry. 2003 Mar 18;42(10):2816–24.
Engstrom, Gregory, et al. “Design of a ruthenium-labeled cytochrome c derivative to study electron transfer with the cytochrome bc1 complex.Biochemistry, vol. 42, no. 10, Mar. 2003, pp. 2816–24. Pubmed, doi:10.1021/bi027213g.
Engstrom G, Rajagukguk R, Saunders AJ, Patel CN, Rajagukguk S, Merbitz-Zahradnik T, Xiao K, Pielak GJ, Trumpower B, Yu C-A, Yu L, Durham B, Millett F. Design of a ruthenium-labeled cytochrome c derivative to study electron transfer with the cytochrome bc1 complex. Biochemistry. 2003 Mar 18;42(10):2816–2824.
Journal cover image

Published In

Biochemistry

DOI

ISSN

0006-2960

Publication Date

March 18, 2003

Volume

42

Issue

10

Start / End Page

2816 / 2824

Location

United States

Related Subject Headings

  • Saccharomyces cerevisiae Proteins
  • Ruthenium
  • Photolysis
  • Osmolar Concentration
  • Organometallic Compounds
  • Models, Chemical
  • Kinetics
  • Heme
  • Electron Transport Complex III
  • Electron Transport