Publications
The sole tryptophan of amicyanin enhances its thermal stability but does not influence the electronic properties of the type 1 copper site. Arch Biochem Biophys. 550-551, 20-7
(2014) Site-directed mutagenesis of proline 52 to glycine in amicyanin converts a true electron transfer reaction into one that is conformationally gated. Biochemistry. 45, 8284-93
(2006) Replacement of the axial copper ligand methionine with lysine in amicyanin converts it to a zinc-binding protein that no longer binds copper. J Inorg Biochem. 105, 1638-44
(2011) Proline 96 of the copper ligand loop of amicyanin regulates electron transfer from methylamine dehydrogenase by positioning other residues at the protein-protein interface. Biochemistry. 50, 1265-73
(2011) Generation of novel copper sites by mutation of the axial ligand of amicyanin. Atomic resolution structures and spectroscopic properties. Biochemistry. 46, 1900-12
(2007) (2009) (2006)