Loop-contraction mutagenesis of a type 1 copper site.
Loop-contraction mutagenesis has been applied to the cupredoxin pseudoazurin to introduce the active-site loop of amicyanin. The mutation has a limited effect on the spectroscopic properties, and therefore structure, of the cupric protein. The loop contraction results in the increase of the pKa for the detachable His ligand of pseudoazurin by two pH units, similar to the value as found in amicyanin.
Yanagisawa
Sachiko
S
School of Natural Sciences, Bedson Building, University of Newcastle upon Tyne, Newcastle upon Tyne NE1 7RU, UK.
Dennison
Christopher
C
D000421:Alcaligenes / Q000737:chemistry; D001400:Azurin / Q000031:analogs & derivatives* / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry*; D001665:Binding Sites; D003300:Copper / Q000737:chemistry*; D004578:Electron Spin Resonance Spectroscopy; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008667:Metalloproteins / Q000737:chemistry*; D016296:Mutagenesis; D010231:Paracoccus denitrificans / Q000737:chemistry; D011487:Protein Conformation; D013056:Spectrophotometry, Ultraviolet; D013329:Structure-Activity Relationship
D001426:Bacterial Proteins; D008667:Metalloproteins; C050107:cupredoxin; C017079:mauC protein, Methylobacterium extorquens; C047163:pseudoazurin; D001400:Azurin; D003300:Copper