Additions and corrections
Atrazine transformation using synthetic enzymes prepared by molecular imprinting
Toshifumi Takeuchi, Satoshi Ugata, Shuichi Masuda, Jun Matsui and Masayoshi Takase
Organic & Biomolecular Chemistry, 2004, 2, 2563–2566 (DOI: 10.1039/b407002j) Amendment published 8th September 2004
One author's name was omitted from the author list. The correct list should read:
Toshifumi Takeuchi,*ab Satoshi Ugata,c Shuichi Masuda,c Jun Matsui,c Takehisa Yanea and Masayoshi Takaseb
Atrazine transformation using synthetic enzymes prepared by molecular imprinting
Toshifumi Takeuchi, Satoshi Ugata, Shuichi Masuda, Jun Matsui and Masayoshi Takase
Organic & Biomolecular Chemistry, 2004, 2, 2563–2566 (DOI: 10.1039/b407002j) Amendment published 6th February 2006
The authors regret the following errors in the Results and Discussion section:
Vmax and kcat should be 1.0 × 10–6 M min–1 and 1.9 × 10−3 min–1 respectively.
The caption for Fig. 5 should be ‘Effects of substrate concentrations on the atraton production (a) and Lineweaver–Burk plot (b) in IP(S2M6): Vmax = 1.0 × 10−6 M min−1, Km = 5.2 × 10−4 M, [E]total = 5.4 × 10−4 M, kcat=Vmax/[E]total= 1.9 × 10−3 min−1.’
The estimate of k′cat should be 4.1 × 10−4 min−1 and the ratio of the two kcat was evaluated to be at least 4.6.
The caption for Fig. 6 should be ‘Effects of substrate concentrations on atraton production (a) and Lineweaver–Burk plot (b) in free SEMA: V′max = 2.4 × 10−7 M min−1, K′m = 3.1 × 10−4 M, [E]′total = 5.9 × 10−4 M, k′cat = V′max/[E]′total = 4.1 × 10−4 min−1.’
The dissociation constant for the enzyme-inhibitor complex should be 4.7 × 10−5 M, both in the text and in the caption for Fig 7.
The Royal Society of Chemistry apologises for this error and any consequent inconvenience to authors and readers.