Protein interaction sites obtained via sequence homology. The site of complexation of electron transfer partners of cytochrome c revealed by mapping amino acid substitutions onto three-dimensional protein surfaces

Author:

Meyer T.E.,Tollin G.,Cusanovich M.A.

Publisher

Elsevier BV

Subject

General Medicine,Biochemistry

Reference65 articles.

1. Cytochromes c. Biological Aspects;Pettigrew,1987

2. Use of laser flash photolysis time-resolved spectrophotometry to investigate interprotein and intraprotein electron transfer mechanisms;Tollin;Biophysical Chem,1993

3. Crystal structure of a complex between electron transfer partners, cytochrome c peroxidase and cytochrome c;Pelletier;Science,1992

4. Preliminary crystal structure studies of a ternary electron transfer complex between a quinoprotein, a blue copper protein, and a c-type cytochrome;Chen;Protein Sci,1993

5. Redox pathways in electron-transfer proteins: correlations between reactivities, solvent exposure, and unpaired-spin-density;Tollin,1986

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