Inter-Protein Electron Transfer Subgroup

The inter-protein electron transfer (ET) subgroup aims to study the fundamental structural, dynamic, and energetic features that control the protein-protein electron transfer kinetics and the relationship between binding and reactivity.

Mixed Metal Hemoglobin Hybrids

Mixed metal hemoglobin hybrids are used as a “predocked” complex to explore the effects of the material environment upon ET.

Cytochrome c Peroxidase and Cytochrome c

Cytochrome c peroxidase (CcP) and cytochrome c (Cyt c) are used as a model system for proteins with multiple binding domains to study complex kinetics.

The W191F mutation of CcP eliminates the redox active tryptophan and allows direct heme-heme electron-transfer.

Project Collaborators: Prof. Marcellus Ubbink (Leiden University)

Myoglobin and Cytochrome b5

Myoglobin (Mb) and cytochrome b5 (b5) constitute a model system for the 'dynamic docking’ paradigm

D44

 

E85

 

Oval: Oval: Oval:

D60

 

Oval:

A heme propionate

Myoglobin (Mb)

Cytochrome b5 (b5)

Mutagenesis and heme esterification (dme) increases reactivity and binding between Mb and b5

amipaperrev

kb

 

Different viscogen concentrations

 

Different temperatures

kt

Right Bracket: Right Bracket:

Mb

 

Mb(dme)

 

Zn

Fe

Project Collaborators: Prof. Amy Rosenzweig (NU) and Prof. Michael Wasielewski (NU)

Funding

Illinois Department of Public Health

Molecular Biophysics Training Program

The Hoffman Group