Gated electron transfer as a probe of the configurational dynamics of peptide-protein complexes

Liu Liu; Jing Hong; Michael Y Ogawa

doi:10.1021/ja036579t

Gated electron transfer as a probe of the configurational dynamics of peptide-protein complexes

J Am Chem Soc. 2004 Jan 14;126(1):50-1. doi: 10.1021/ja036579t.

Authors

Liu Liu¹, Jing Hong, Michael Y Ogawa

Affiliation

¹ Department of Chemistry and Center for Photochemical Sciences, Bowling Green State University, Bowling Green, Ohio 43403, USA.

PMID: 14709054
DOI: 10.1021/ja036579t

Abstract

Gated electron-transfer measurements are used to probe the configurational dynamics of complexes formed between small metallopeptides and cytochrome c. The results show that that an apparently subtle chemical alteration of the metallopeptide produces significant changes to the dynamics of the peptide-protein complex.

Publication types

Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.

MeSH terms

2,2'-Dipyridyl / chemistry
Kinetics
Metalloproteins / chemistry*
Phenanthrolines / chemistry
Polyglutamic Acid / chemistry*
Protein Conformation
Ruthenium / chemistry*
Thermodynamics

Substances

Metalloproteins
Phenanthrolines
Polyglutamic Acid
2,2'-Dipyridyl
Ruthenium

Grants and funding

GM61171/GM/NIGMS NIH HHS/United States