NDLI: Selective Examination of Heme Protein Azide Ligand-Distal Globin Interactions by Vibrational Circular Dichroism

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Selective Examination of Heme Protein Azide Ligand-Distal Globin Interactions by Vibrational Circular Dichroism

Content Provider	Semantic Scholar
Author	Bormett, Richard W. Asher, Sanford A. Larkin, Peter J. Gustafson, William G. Ragunathan, Nilusha Freedman, Teresa B. Nafie, Laurence A. Sriram Balasubramanian Boxer, Steven G. Yu, Nai-Teng Gersonde, Klaus Noble, Robert W. Sligar, Stephen G.
Copyright Year	1992
Abstract	Vibrational circular dichroism (VCD) spectra of the antisymmetric stretch of azide ligated to the heme of a series of evolutionarily diverse and site-directed mutant hemoglobins and myoglobins are anomalously intense and demonstrate an intriguing sensitivity to subtle protein-ligand interactions. The antisymmetric stretch of the azide ligand covalently bound to the low-spin iron shows an anisotropy ratio of -9.5 X 10"4 for sperm whale and horse myoglobin which decreases to -8.0 X 10"4 for human and carp hemoglobin and Chironimus thummi thummi III monomeric hemoglobin. The VCD spectra of these heme-azide complexes depend upon the interactions of the azide ligand with distal heme pocket residues such as the E7 distal histidine and El 1 valine. The site-directed mutants of sperm whale (distal histidine substituted GIy E7) and human (distal valine substituted Asn El 1) myoglobin have vanishingly small anisotropy ratios (<-0.5 X 1(T 4), while elephant myoglobin (distal histidine substituted GIn E7) shows an anisotropy ratio of-6.4 X ICT 4. The azide ligand ionically bound to a high-spin iron shows a vanishingly small VCD intensity.
Starting Page	6864
Ending Page	6867
Page Count	4
File Format	PDF HTM / HTML
DOI	10.1021/ja00043a035
Alternate Webpage(s)	http://web.stanford.edu/group/boxer/papers/paper96.pdf
Alternate Webpage(s)	https://doi.org/10.1021/ja00043a035
Volume Number	114
Language	English
Access Restriction	Open
Content Type	Text
Resource Type	Article

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