The 'prismane' protein resolved: X-ray structure at 1.7 Å and multiple spectroscopy of two novel 4Fe clusters

Alexander F. Arendsen, Jonathan Hadden, Graeme Card, Alan S. McAlpine, Susan Bailey, Vjacheslav Zaitsev, Elizabeth H.M. Duke, Peter F. Lindley*, Monika Kröckel, Alfred X. Trautwein, Martinus C. Feiters, John M. Charnock, C. David Garner, Sophie J. Marritt, Andrew J. Thomson, Ingeborg M. Kooter, Michael K. Johnson, Willy A.M. Van Den Berg, Walter M.A.M. Van Dongen, Wilfred R. Hagen

*Corresponding author for this work
62 Citations (Scopus)


The three-dimensional structure of the native 'putative prismane' protein from Desulfovibrio vulgaris (Hildenborough) has been solved by X-ray crystallography to a resolution of 1.72 Å. The molecule does not contain a [6Fe-6S] prismane cluster, but rather two 4Fe clusters some 12 Å apart and situated close to the interfaces formed by the three domains of the protein. Cluster 1 is a conventional [4Fe-4S] cubane bound, however, near the N- terminus by an unusual, sequential arrangement of four cysteine residues (Cys 3, 6, 15, 21). Cluster 2 is a novel 4Fe structure with two μ2-sulfido bridges, two μ2-oxo bridges, and a partially occupied, unidentified μ2 bridge X. The protein ligands of cluster 2 are widely scattered through the second half of the sequence and include three cysteine residues (Cys 312, 434, 459), one persulfido-cysteine (Cys 406), two glutamates (Glu 268, 494), and one histidine (His 244). With this unusual mixture of bridging and external type of ligands, cluster 2 is named the 'hybrid' cluster, and its asymmetric, open structure suggests that it could be the site of a catalytic activity. X-ray absorption spectroscopy at the Fe K-edge is readily interpretable in terms of the crystallographic model when allowance is made for volume contraction at 10K; no Fe··Fe distances beyond 3.1 Å could be identified. EPR, Mossbauer and MCD spectroscopy have been used to define the oxidation states and the magnetism of the clusters in relation to the crystallographic structure. Reduced cluster 1 is a [4Fe-4S]1+ cubane with S = 3/2; it is the first biological example of a 'spin-admixed' iron-sulfur cluster. The hybrid cluster 2 has four oxidation states from (formally) all Fe(III) to three Fe(II) plus one Fe(III). The four iron ions are exchange coupled resulting in the system spins S = 0, 9/2, 0 (and 4), 1/2, respectively for the four redox states. Resonance Raman spectroscopy suggests that the bridging ligand X which could not be identified unambiguously in the crystal structure is a solvent-exchangeable oxygen.

Original languageEnglish
JournalJournal of Biological Inorganic Chemistry
Issue number1
Pages (from-to)81-95
Number of pages15
Publication statusPublished - 01.02.1998


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