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Nature Chemical Biology 1, 6 - 7 (2005)
doi:10.1038/nchembio0605-6
Pulling NO out of thin air
Thomas G Spiro1
- Thomas G. Spiro is in the Department of Chemistry, Princeton University, Princeton, New Jersey 08544, USA. e-mail: spiro@princeton.edu
Abstract
Nitric oxide signaling requires that the heme of soluble guanylate cyclase bind NO preferentially to O2. Engineering of the enzyme's active site reveals a molecular basis for NO binding selectivity.
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A molecular basis for NO selectivity in soluble guanylate cyclaseNature Chemical Biology Article (01 Jun 2005)
NO and CO differentially activate soluble guanylyl cyclase via a heme pivot-bend mechanismThe EMBO Journal Article (24 Jan 2007)
Unprecedented proximal binding of nitric oxide to heme: implications for guanylate cyclaseThe EMBO Journal Article (01 Nov 2000)

