English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Conformational changes in cytochrome c and cytochrome oxidase upon complex formation: A resonance Raman study.

Hildebrandt, P., Heimburg, T., Marsh, D., & Powell, G. L. (1990). Conformational changes in cytochrome c and cytochrome oxidase upon complex formation: A resonance Raman study. Biochemistry, 29(6), 1661-1668. doi:10.1021/bi00458a044.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0013-0E40-D Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-32FD-E
Genre: Journal Article

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Hildebrandt, P.1, Author              
Heimburg, T.2, Author              
Marsh, D.1, Author              
Powell, G. L., Author
Affiliations:
1Department of Spectroscopy and Photochemical Kinetics, MPI for biophysical chemistry, Max Planck Society, ou_578624              
2Research Group of Biophysics and Thermodynamics of Membranes, MPI for biophysical chemistry, Max Planck Society, ou_578546              

Content

show
hide
Free keywords: -
 Abstract: The fully oxidized complex of cytochrome c and cytochrome oxidase formed at low ionic strength was studied by resonance Raman spectroscopy. The spectra of the complex and of the individual components were compared over a wide frequency range using Soret band excitation. In both partners of the complex, structural changes occur in the heme groups and in their immediate protein environment. The spectra of the complex in the 1600-1700 cm-1 frequency range were dominated by bands from the cytochrome oxidase component, whereas those in the 300-500 cm-1 range were dominated by bands from the cytochrome c component, hence allowing separation of the contributions from the two individual species. For cytochrome c, spectral changes were observed which correspond to the induction of the conformational state I and the six-coordinated low-spin configuration of state II on binding to cytochrome oxidase. While in state I the structure of cytochrome c is essentially the same as in solution, state II is characterized by a structural rearrangement of the heme pocket, leading to a weakening of the axial iron-methionine bond and an opening of the heme crevice which is situated in the center of the binding domain for cytochrome oxidase. The relative contributions of the two cytochrome c states were estimated to be approximately in the ratio 1:1 in the complex.

Details

show
hide
Language(s): eng - English
 Dates: 1990-02-13
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1021/bi00458a044
ISI: A1990CN39400044
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Biochemistry
  Alternative Title : Biochemistry
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 29 (6) Sequence Number: - Start / End Page: 1661 - 1668 Identifier: ISSN: 0006-2960