A molecular basis for NO selectivity in soluble guanylate cyclase
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Molecular Biology
Link
http://www.nature.com/articles/nchembio704z.pdf
Reference31 articles.
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2. Iyer, L.M., Anantharaman, V. & Aravind, L. Ancient conserved domains shared by animal soluble guanylyl cyclases and bacterial signaling proteins. BMC Genomics 4, 5 (2003).
3. Karow, D.S. et al. Spectroscopic characterization of the soluble guanylate cyclase-like heme domains from Vibrio cholerae and Thermoanaerobacter tengcongensis . Biochemistry 43, 10203–10211 (2004).
4. Pellicena, P. et al. Crystal structure of an oxygen-binding heme domain related to soluble guanylate cyclases. Proc. Natl. Acad. Sci. USA 101, 12854–12859 (2004).
5. Mathews, A.J. & Olson, J.S. Assignment of rate constants for O2 and CO binding to α-subunit and β-subunit within R-state and T-state human hemoglobin. Methods Enzymol. 232, 363–386 (1994).
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