Ligand binding to cytochrome c and other related haem proteins and peptides. Part I. Equilibrium studies |
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| Affiliation: | 1. Department of Geomatics, Forest Research Institute, Sękocin Stary, 05-090 Raszyn, Poland;2. Department of Forest Management, Geomatics and Forest Economics, Faculty of Forestry, Warsaw University of Life Sciences – SGGW, Warsaw, 02-776 Warsaw, Poland;1. Department of Applied Ecology, Box 7617, North Carolina State University, Raleigh, NC 27695, USA;2. U.S. Environmental Protection Agency, 77 West Jackson Blvd., Chicago, IL 60604, USA;3. Department of Biology, 901 South Avenue, Missouri State University, Springfield, MO 65897, USA;4. Warnell School of Forestry and Natural Resources, University of Georgia, 180 East Green Street, Athens, GA 30602, USA |
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| Abstract: | Investigation of ligand binding to native cytochrome c, carboxymethyl-Met 80-cytochrome c, myoglobin and haemhexapeptide revealed that the binding of exogenous ligands is modulated by the following factors: - 1.Hydrophobicity of the haem environment.
- 2.Haem accessibility to exogenous ligands, termed the haem crevice ‘open-closed’ parameter.
- 3.Steric interactions between the protein and the bound ligand.
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