1E84
Cytochrome c' from Alcaligenes xylosoxidans - reduced structure
Summary for 1E84
| Entry DOI | 10.2210/pdb1e84/pdb |
| Related | 1CGO 1E83 1E85 1E86 |
| Descriptor | CYTOCHROME C', HEME C (3 entities in total) |
| Functional Keywords | cytochrome, heme, 4-helix bundle, electron transport |
| Biological source | ALCALIGENES XYLOSOXIDANS |
| Total number of polymer chains | 1 |
| Total formula weight | 14249.94 |
| Authors | Lawson, D.M.,Stevenson, C.E.M.,Andrew, C.R.,Eady, R.R. (deposition date: 2000-09-15, release date: 2000-11-06, Last modification date: 2024-10-16) |
| Primary citation | Lawson, D.M.,Stevenson, C.E.M.,Andrew, C.R.,Eady, R.R. Unprecedented Proximal Binding of Nitric Oxide to Heme: Implications for Guanylate Cyclase Embo J., 19:5661-, 2000 Cited by PubMed 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 with dioxygen. We report the 1.95 and 1.35 A resolution crystal structures 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 binds 6-coordinate on the distal side. A second CO molecule, not bound to the 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. PubMed: 11060017DOI: 10.1093/EMBOJ/19.21.5661 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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