Unprecedented proximal binding of nitric oxide to heme: implications for guanylate cyclase

Citation
Dm. Lawson et al., Unprecedented proximal binding of nitric oxide to heme: implications for guanylate cyclase, EMBO J, 19(21), 2000, pp. 5661-5671
Citations number
54
Categorie Soggetti
Molecular Biology & Genetics
Journal title
EMBO JOURNAL
ISSN journal
02614189 → ACNP
Volume
19
Issue
21
Year of publication
2000
Pages
5661 - 5671
Database
ISI
SICI code
0261-4189(20001101)19:21<5661:UPBONO>2.0.ZU;2-N
Abstract
Microbial cytochromes c' contain a 5-coordinate His-ligated heme that forms stable adducts with nitric oxide (NO) and carbon monoxide (CO), but not wi th dioxygen, We report the 1.95 and 1.35 Angstrom resolution crystal struct ures of the CO- and NO-bound forms of the reduced protein from Alcaligenes xylosoxidans, NO disrupts the His-Fe bond and binds in a novel mode to the proximal face of the heme, giving a 5-coordinate species. In contrast, CO b inds 6-coordinate on the distal side. A second CO molecule, not bound to th e heme, is located in the proximal pocket. Since the unusual spectroscopic properties of cytochromes c' are shared by soluble guanylate cyclase (sGC), our findings have potential implications for the activation of sGC induced by the binding of NO or CO to the heme domain.