The effect of complex formation upon the reduction rates of cytochrome c and cytochrome c peroxidase compound II

1987 ◽  
Vol 913 (3) ◽  
pp. 257-271 ◽  
Author(s):  
Peter Cokie ◽  
James E. Erman
Keyword(s):  
Cytochrome C ◽  
Complex Formation ◽  
Cytochrome C Peroxidase ◽  
Compound Ii

Role of methionine 230 in intramolecular electron transfer between the oxyferryl heme and tryptophan 191 in cytochrome c peroxidase compound II

Biochemistry ◽  
1994 ◽  
Vol 33 (29) ◽  
pp. 8678-8685 ◽  
Author(s):  
Rui-Qin Liu ◽  
Mark A. Miller ◽  
Gye Won Han ◽  
Seung Hahm ◽  
Lois Geren ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Cytochrome C ◽  
Cytochrome C Peroxidase ◽  
Intramolecular Electron Transfer ◽  
Compound Ii

scholarly journals Nε,Nε-Dimethyl-lysine cytochrome c as an NMR probe for lysine involvement in protein–protein complex formation

1998 ◽  
Vol 332 (2) ◽  
pp. 439-449 ◽  
Author(s):  
Geoffrey R. MOORE ◽  
Mark C. COX ◽  
David CROWE ◽  
Michael J. OSBORNE ◽  
Federico I. ROSELL ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Complex Formation ◽  
Protein Complex ◽  
Brownian Dynamics ◽  
Chemical Exchange ◽  
Cytochrome B5 ◽  
Cytochrome C Peroxidase ◽  
Bovine Liver ◽  
13C Nmr Spectroscopy ◽  
Protein Complex Formation

The reductively dimethylated derivatives of horse and yeast iso-1-ferricytochromes c have been prepared and characterized for use as NMR probes of the complexes formed by cytochrome c with bovine liver cytochrome b5 and yeast cytochrome c peroxidase. The electrostatic properties and structures of the derivatized cytochromes are not significantly perturbed by the modifications; neither are the electrostatics of protein–protein complex formation or rates of interprotein electron transfer. Two-dimensional 1H–13C NMR spectroscopy of the complexes formed by the derivatized cytochromes with cytochrome b5 and cytochrome c peroxidase has been used to investigate the number and identity of lysine residues of cytochrome c that are involved in interprotein interactions of cytochrome c. The NMR data are incompatible with simple static models proposed previously for the complexes formed by these proteins, but are consistent with the presence of multiple, interconverting complexes of comparable stability, consistent with studies employing Brownian dynamics to model the complexes. The NMR characteristics of the Nε,Nε-dimethyl-lysine groups, their chemical shift dispersion, oxidation state and temperature dependences and the possibility of chemical exchange phenomena are discussed with relevance to the utility of Nε,Nε-dimethyl-lysine's being a generally useful derivative for characterizing protein–protein complexes.

scholarly journals Efficient Encounter Complex Formation and Electron Transfer to Cytochrome  c Peroxidase with an Additional, Distant Electrostatic Binding Site

2020 ◽  
Vol 59 (51) ◽  
pp. 23239-23243
Author(s):  
Antonella Di Savino ◽  
Johannes M. Foerster ◽  
Thijmen La Haye ◽  
Anneloes Blok ◽  
Monika Timmer ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Cytochrome C ◽  
Complex Formation ◽  
Binding Site ◽  
Cytochrome C Peroxidase ◽  
Encounter Complex ◽  
Electrostatic Binding

A rapid-scan spectrometric and stopped-flow study of Compound I and Compound II of Pseudomonas cytochrome c peroxidase

1985 ◽  
Vol 236 (2) ◽  
pp. 714-719 ◽  
Author(s):  
Marjaana Rönnberg ◽  
Anne-Marie Lambeir ◽  
Nils Ellfolk ◽  
H.Brian Dunford
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Peroxidase ◽  
Stopped Flow ◽  
Compound I ◽  
Rapid Scan ◽  
Compound Ii ◽  
Flow Study

scholarly journals Efficient Encounter Complex Formation and Electron Transfer to Cytochrome  c Peroxidase with an Additional, Distant Electrostatic Binding Site

2020 ◽  
Vol 132 (51) ◽  
pp. 23439-23443
Author(s):  
Antonella Di Savino ◽  
Johannes M. Foerster ◽  
Thijmen La Haye ◽  
Anneloes Blok ◽  
Monika Timmer ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Cytochrome C ◽  
Complex Formation ◽  
Binding Site ◽  
Cytochrome C Peroxidase ◽  
Encounter Complex ◽  
Electrostatic Binding

The Dynamics and Oxidation State Dependence of Complex Formation between Cytochrome C Peroxidase and Cytochrome C

1991 ◽  
Vol 194 (1) ◽  
pp. 351-356 ◽  
Author(s):  
Richard Hake ◽  
Qipan Zhang ◽  
John Marohn ◽  
George McLendon ◽  
Alan Corin
Keyword(s):  
Cytochrome C ◽  
Complex Formation ◽  
Oxidation State ◽  
Cytochrome C Peroxidase ◽  
State Dependence
Sign in / Sign up

Export Citation Format

Share Document