title: Gated electron transfer as a probe of the configurational dynamics of peptide-protein complexes.
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.
authors.affiliation: Department of Chemistry and Center for Photochemical Sciences, Bowling Green State University, Bowling Green, Ohio 43403, USA.
authors.forename: Liu
authors.initials: L
authors.lastname: Liu
authors.forename: Jing
authors.initials: J
authors.lastname: Hong
authors.forename: Michael Y
authors.initials: MY
authors.lastname: Ogawa
mesh_terms: D015082:2,2'-Dipyridyl / Q000737:chemistry; D007700:Kinetics; D008667:Metalloproteins / Q000737:chemistry*; D010618:Phenanthrolines / Q000737:chemistry; D011099:Polyglutamic Acid / Q000737:chemistry*; D011487:Protein Conformation; D012428:Ruthenium / Q000737:chemistry*; D013816:Thermodynamics
chemical_list: D008667:Metalloproteins; D010618:Phenanthrolines; D011099:Polyglutamic Acid; D015082:2,2'-Dipyridyl; D012428:Ruthenium