Determinants of the Relative Reduction Potentials of Type-1 Copper Sites in Proteins

Citations Over TimeTop 10% of 2004 papers

Abstract

The relative Cu(2+)/Cu(+) reduction potentials of six type-1 copper sites (cucumber stellacyanin, P. aeruginosa azurin, poplar plastocyanin, C. cinereus laccase, T. ferrooxidans rusticyanin, and human ceruloplasmin), which lie in a reduction potential range from 260 mV to over 1000 mV, have been studied by quantum mechanical calculations. The range and relative orderings of the reduction potentials are reproduced very well compared to experimental values. The study suggests that the main structural determinants of the relative reduction potentials of the blue copper sites are located within 6 A of the Cu atoms. Further analysis suggests that the reduction potential differences of type-1 copper sites are caused by axial ligand interactions, hydrogen bonding to the S(Cys), and protein constraint on the inner sphere ligand orientations. The low reduction potential of cucumber stellacyanin is due mainly to a glutamine ligand at the axial position, rather than a methionine or a hydrophobic residue as in the other proteins. A stronger interaction with a backbone carbonyl group is a prime contributor to the lower reduction potential of P. aeruginosa azurin as compared to poplar plastocyanin, whereas the reverse is true for C. cinereus laccase and T. ferrooxidans rusticyanin. The lack of an axial methonine ligand also contributes significantly to the increased reduction potentials of C. cinereus laccase and human ceruloplasmin. However, in the case of C. cinereus laccase, this increase is attenuated by the presence of only one amide NH hydrogen bond to the S(Cys) rather than two in the other proteins. In human ceruloplasmin the reduction potential is further increased by the structural distortion of the equatorial ligand orientation.

Related Papers

• → Gene synthesis, expression, and mutagenesis of the blue copper proteins azurin and plastocyanin.(1991)60 cited
• → Interaction of cytochrome c with the blue copper proteins, plastocyanin and azurin.(1983)47 cited
• → Structure and Electron Transfer Reactions of Blue Copper Proteins(1977)4 cited
• Preferred sites and pathways for electron transfer in blue copper proteins.(1988)
• → ChemInform Abstract: KINETIC STUDIES OF 1:1 ELECTRON‐TRANSFER REACTIONS INVOLVING BLUE COPPER PROTEINS. PART 10. THE ASSIGNMENT OF BINDING SITES IN THE REACTIONS OF PLASTOCYANIN (AND AZURIN) WITH NONPHYSIOLOGICAL PROTEIN REDOX PARTNERS(1985)