Published December 1992
| public
Journal Article
Blue to type 2 binding. Copper(II) and cobalt(II) derivatives of a Cys112Asp mutant of Pseudomonas aeruginosa azurin
Abstract
Of the five invariant residues that surround the copper in azurins, the ligand cysteine at position 112 (Cys112) is believed to be especially important in the bonding interactions responsible for the unusual blue copper absorption and electron paramagnetic resonance (EPR) spectra. It is striking that mutagenesis studies of Met121, His46, and His174 ave shown that these ligands are not required for a blue copper center, thereby reinforcing the feeling that Cys112 is absolutely essential. To address this issue directly, we have replaced Cys112 with Asp by site-directed mutagenesis.
Additional Information
© 1992 American Chemical Society. Received June 29, 1992. We thank Dr. David B. Goodin of the Scripps Research Institute for assistance with the EPR measurements. This work was supported by grants from the National Institutes of Health (DK19038 to H.B.G.; GM16424 to J.H.R.; GM07616 traineeship to T.J.M.).Additional details
- Eprint ID
- 57194
- Resolver ID
- CaltechAUTHORS:20150504-113949666
- DK19038
- NIH
- GM16424
- NIH
- GM07616
- NIH
- Created
-
2015-05-04Created from EPrint's datestamp field
- Updated
-
2021-11-10Created from EPrint's last_modified field
- Other Numbering System Name
- Caltech Division of Chemistry and Chemical Engineering
- Other Numbering System Identifier
- 8671