Conformational Dependence of Electron Transfer across de novo Designed Metalloproteins

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 93; no. 18; pp. 9521 - 9526
• Main Authors: Mutz, Mitchell W., McLendon, George L., Wishart, James F., Gaillard, Elizabeth R., Corin, Alan F.
• Format: Journal Article
• Language: English
• Published: United States National Academy of Sciences of the United States of America 03.09.1996; National Acad Sciences; National Academy of Sciences
• Subjects: Amino Acid Sequence; Biochemistry; Chemistry; Circular Dichroism; Drug Design; Electrodes; Electron transfer; Electron Transport; Electrons; Metalloproteins; Metalloproteins - chemistry; Molecular Sequence Data; Phosphates; Photolysis; Protein Conformation; Proteins; Radiolysis; Sodium; Viologens; Voltammetry
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.93.18.9521

Flash photolysis and pulse radiolysis measurements demonstrate a conformational dependence of electron transfer rates across a 16-mer helical bundle (three-helix metalloprotein) modified with a capping CoIII(bipyridine)3 electron acceptor at the N terminus and a 1-ethyl-1′-ethyl-4,4′-bip yridinium donor at the C terminus. For the CoIII(peptide)3-1-ethyl-1<la tex>$^{\prime}$ -ethyl-4,4′-bipyridinium maquettes, the observed transfer is a first order, intramolecular process, independent of peptide concentration or laser pulse energy. In the presence of 6 M urea, the random coil bundle (≈ 0% helicity) has an observed electron transfer rate constant of kobs = 900 ± 100 s-1. In the presence of 25% trifluoroethanol (TFE), the helicity of the peptide is 80% and the kobs increases to 2000 ± 200 s-1. Moreover, the increase in the rate constant in TFE is consistent with the observed decrease in donor--acceptor distance in this solvent. Such bifunctional systems provide a class of molecules for testing the effects of conformation on electron transfer in proteins and peptides.