Effects of surface amino acid replacements in cytochrome c peroxidase on complex formation with cytochrome c

Biochemistry ◽  
1991 ◽  
Vol 30 (49) ◽  
pp. 11585-11595 ◽  
Author(s):  
Alan F. Corin ◽  
George McLendon ◽  
Qipan Zhang ◽  
Richard A. Hake ◽  
Joseph Falvo ◽  
...  
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Complex Formation ◽  
Cytochrome C Peroxidase

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

scholarly journals Pseudomonas Cytochrome c Peroxidase. VIII. The Amino Acid Composition of the Enzyme.

1973 ◽  
Vol 27 ◽  
pp. 2193-2198 ◽  
Author(s):  
Ritva Soininen ◽  
Nils Ellfolk ◽  
Ritva Soininen ◽  
Jacques M. Waisvisz ◽  
Marcel G. van der Hoeven ◽  
...  
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Cytochrome C Peroxidase

Effects of surface amino acid replacements in cytochrome c peroxidase on intracomplex electron transfer from cytochrome c

Biochemistry ◽  
1993 ◽  
Vol 32 (11) ◽  
pp. 2756-2762 ◽  
Author(s):  
Alan F. Corin ◽  
Richard A. Hake ◽  
George McLendon ◽  
James T. Hazzard ◽  
Gordon Tollin
Keyword(s):  
Electron Transfer ◽  
Amino Acid ◽  
Cytochrome C ◽  
Cytochrome C Peroxidase

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
Sign in / Sign up

Export Citation Format

Share Document