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Crystallographic analysis of the intact metal centres [3Fe–4S] 1+/0 and [4Fe–4S] 2+/1+ in a Zn 2+ ‐containing ferredoxin
Author(s) -
Frazão Carlos,
Aragão David,
Coelho Ricardo,
Leal Sónia S.,
Gomes Cláudio M.,
Teixeira Miguel,
Carrondo Maria Arménia
Publication year - 2008
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2008.01.041
Subject(s) - ferredoxin , crystallography , chemistry , cluster (spacecraft) , crystal structure , metal , folding (dsp implementation) , biochemistry , enzyme , organic chemistry , computer science , electrical engineering , programming language , engineering
Detailed structural models of di‐cluster seven‐iron ferredoxins constitute a valuable resource for folding and stability studies relating the metal cofactors’ role in protein stability. The here reported, hemihedric twinned crystal structure at 2.0 Å resolution from Acidianus ambivalens ferredoxin, shows an integral 103 residues, physiologically relevant native form composed by a N‐terminal extension comprising a His/Asp Zn 2+ site and the ferredoxin (βαβ) 2 core, which harbours intact clusters I and II, a [3Fe–4S] 1+/0 and a [4Fe–4S] 2+/1+ centres. This is in contrast with the previously available ferredoxin structure from Sulfolofus tokodai , which was obtained from an artificial oxidative conversion with two [3Fe–4S] 1+/0 centres and poor definition around cluster II.