Structure and electrochemistry of oxidoreductases.
The principles on which Nature has developed multifunctional redox centres, covering a large range of potentials, protected from water and oxygen and surrounded by highly specific proteins, are demonstrated. Structures and accessibilities of the active sites of iron-sulphur proteins, sulphur proteins, flavoproteins, cytochromes and copper proteins are correlated with their possibilities and modes of electron exchange with natural partners, artificial mediators and (modified) electrodes. The participation of charge-transfer and tunnelling processes in electron transport is demonstrated, and a suitable relative orientation of the partners is recognized as one of the most important requirements for electrochemical communication between large molecules and electrodes. The use of specifically modified electrode surfaces, for example those based on electroconductive polymers, is proposed as one of the aspects of future developments for direct electron transfer to proteins.
D003580:Cytochromes / Q000378:metabolism; D004563:Electrochemistry; D004579:Electron Transport; D005420:Flavoproteins / Q000378:metabolism; D007506:Iron-Sulfur Proteins / Q000378:metabolism; D008667:Metalloproteins / Q000378:metabolism; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000378:metabolism*; D011166:Porphyrins / Q000378:metabolism
D003580:Cytochromes; D005420:Flavoproteins; D007506:Iron-Sulfur Proteins; D008667:Metalloproteins; D011166:Porphyrins; D010088:Oxidoreductases