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- W2003448704 abstract "The roles of the Trp144 and Tyr203 residues near the type 1 Cu site of Achromobacter cycloclastes nitrite reductase (AcNIR) have been examined with mutants of AcNIR. Tyr203 is located on the protein surface near the type 1 Cu site of AcNIR, and Trp144 is between the Tyr203 and the type 1 Cu center in AcNIR. Single mutation of Trp144 or Tyr203 in AcNIR to Leu resulted in decreased rate constants of intermolecular electron transfer from its cognate pseudoazurin (AcPAZ) (k(ET)=1.9x10(5), 2.2x10(5), and 7.3x10(5)M(-1)s(-1) for W144L, Y203L, and wild-type AcNIR, respectively). The intermolecular electron transfer rate constant of double mutant AcNIR (W144L/Y203L) was the same as those of single mutants (k(ET)=1.9x10(5)M(-1)s(-1) for W144L/Y203L). The redox potentials, coordination structures of the type 1 Cu, and the enzyme activities of AcNIR were affected little by the mutation." @default.
- W2003448704 created "2016-06-24" @default.
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- W2003448704 date "2005-10-01" @default.
- W2003448704 modified "2023-10-03" @default.
- W2003448704 title "Roles of Trp144 and Tyr203 in copper-containing nitrite reductase from Achromobacter cycloclastes IAM1013" @default.
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- W2003448704 doi "https://doi.org/10.1016/j.bbrc.2005.08.076" @default.
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