title: Use of a tyrosine hydroxylase mutant enzyme with reduced metal affinity allows detection of activity with cobalt in place of iron.
authors.affiliation: Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843-2128, USA.
authors.forename: Holly R
authors.initials: HR
authors.lastname: Ellis
authors.forename: Kevin P
authors.initials: KP
authors.lastname: McCusker
authors.forename: Paul F
authors.initials: PF
authors.lastname: Fitzpatrick
mesh_terms: D001665:Binding Sites; D001671:Biochemistry / Q000379:methods*; D003035:Cobalt / Q000032:analysis / Q000378:metabolism*; D007501:Iron / Q000378:metabolism*; D009154:Mutation; D011622:Pterins / Q000378:metabolism; D013054:Spectrophotometry, Atomic; D014446:Tyrosine 3-Monooxygenase / Q000235:genetics* / Q000378:metabolism*
chemical_list: D011622:Pterins; C011552:tetrahydropterin; D003035:Cobalt; D007501:Iron; D014446:Tyrosine 3-Monooxygenase