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The authors describe their packing-density model for estimating long-range couplings in protein ET reactions. They also provide a steady-state kinetics analysis of multistep tunneling in proteins.
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This brief note illustrates the protein-structure dependence of long-range electronic couplings in Ru-modified high-potential iron-sulfur proteins.
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Babini E., Bertini I., Borsari M., Capozzi F., Luchinat C., Di Bilio A.J., Gray H.B., Ponce A., Winkler J.R. Electron transfer in ruthenium-modified high-potential iron sulfur proteins. J Inorg Biochem. 74:1999;266. This brief note illustrates the protein-structure dependence of long-range electronic couplings in Ru-modified high-potential iron-sulfur proteins.
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The controversy regarding conformational control (i.e. gating) of ET in cytochrome-c/cytochrome-c-peroxidase is addressed in this paper. ET in yeast-yeast pairs is not gated, but it is in the yeast-horse complex.
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Mei H., Wang K., Peffer N., Weatherly G., Cohen D.S., Miller M., Pielak G., Durham B., Millett F. Role of configurational gating in intracomplex electron transfer from cytochrome c to the radical cation in cytochrome c peroxidase. Biochemistry. 38:1999;6846-6854. The controversy regarding conformational control (i.e. gating) of ET in cytochrome-c/cytochrome-c-peroxidase is addressed in this paper. ET in yeast-yeast pairs is not gated, but it is in the yeast-horse complex.
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306 to FADH. Biophys J. 76:1999;1241-1249. This theoretical analysis of ET in Escherichia coli DNA photolyase identifies two Trp residues in the pathway between FADH and Tyr306. The calculations were based on long-range superexchange coupling, but multistep tunneling might be involved as well.
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370 of mouse ribonucleotide reductase protein R2 is the connecting link in the intersubunit radical transfer pathway
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In a model of the R1-R2 protein complex of ribonucleotide reductase, critical residues in the interfacial region were not identified because of disorder in the carboxy-terminal region of the R2 protein. Mutagenesis studies described in this paper identify a critical tyrosine residue as the link in the radical-transfer pathway between the two proteins.
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370 of mouse ribonucleotide reductase protein R2 is the connecting link in the intersubunit radical transfer pathway. J Biol Chem. 274:1999;23746-23751. In a model of the R1-R2 protein complex of ribonucleotide reductase, critical residues in the interfacial region were not identified because of disorder in the carboxy-terminal region of the R2 protein. Mutagenesis studies described in this paper identify a critical tyrosine residue as the link in the radical-transfer pathway between the two proteins.
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Rova, U.1
Adrait, A.2
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Thelander, L.5
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Preserved catalytic activity in an engineered ribonucleotide reductase R2 protein with a nonphysiological radical transfer pathway
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Ekberg M., Pötsch S., Sandin E., Thunissen M., Nordlund P., Sahlin M., Sjöberg B.-M. Preserved catalytic activity in an engineered ribonucleotide reductase R2 protein with a nonphysiological radical transfer pathway. J Biol Chem. 273:1998;21003-21008.
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Ekberg, M.1
Pötsch, S.2
Sandin, E.3
Thunissen, M.4
Nordlund, P.5
Sahlin, M.6
Sjöberg, B.-M.7
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