Crystallographic studies of azide, thiocyanate and perchlorate complexes of methemerythrin. |
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Authors: | R E Stenkamp L C Sieker L H Jensen |
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Affiliation: | Department of Biological Structure and Department of Biochemistry University of Washington, Seattle, WA 98195, U.S.A. |
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Abstract: | Difference Fourier maps of azide, thiocyanate and perchlorate complexes of methemerythrin from Themiste dyscritum have been calculated at 4 Å, 3.5 Å and 3.5 Å resolution, respectively, with phases from a refined model. N?3 and SCN? bind to the Fe complex in each subunit, indicating the mode of oxygen binding and suggesting a possible route followed by the anions in reaching the complex. ClO?4 binds in two different locations on the non-crystallographic 2-fold axes near cysteine 9 and cysteine 50, apparently being held to the protein by peptide amides and lysine side-chains. Binding of ClO?4 at these locations away from the Fe complex is observed to have some effect on the active site structure. |
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