Structural distortions of the [Fe4S4]2+ core of [Fe4S4(S-t-C4H9)4]2− in different crystalline environments and detection and instability of oxidized ([Fe4S4]3+) clusters

Mascharak, P. K.; Hagen, Karl S.; Spence, J. T.; Holm, R. H.

doi:10.1016/s0020-1693(00)91277-5

Cited by 58 publications

(57 citation statements)

References 44 publications

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“…The standard uncertainties in the bond lengths within the H42Q-1 cluster (0.93 A Ê resolution) shown in Table 2 are around 0.004 A Ê , similar to those quoted for the 0.94 A Ê resolution structure of the ferredoxin from Clostridium acidurici (Dauter et al, 1997) (Mascharak et al, 1983), which in both cases were about 0.003 A Ê . As would be expected for the lower resolution (1.20 A Ê ), the standard uncertainties for the rc-WT structure (also shown in Table 2) are a little larger, however if the equivalent distances in the two molecules in the asymmetric unit are averaged, the resulting standard uncertainties are also about 0.004 A Ê .…”

Section: Assessment Of Standard Uncertaintiessupporting

confidence: 77%

“…Studies of model compounds (Averill et al, 1973, Berg & Holm, 1982Mascharak et al, 1983) and of the C. vinosum HiPIP at 2 A Ê resolution (Carter et al, 1972) shown the presence of tetragonally distorted clusters with approximate D 2 d(À42m) symmetry and four short and eight long FeÐS bonds. As can be seen from Table 2, this is also true to a good ®rst approximation for all three independent molecules reported here.…”

Section: Cluster Geometrymentioning

confidence: 98%

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Ab initio solution and refinement of two high-potential iron protein structures at atomic resolution

Parisini

Capozzi

Lubini

et al. 1999

Acta Crystallogr D Biol Cryst

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The crystal structure of the reduced high-potential iron protein (HiPIP) from Chromatium vinosum has been redetermined in a new orthorhombic crystal modi®cation, and the structure of its H42Q mutant has been determined in orthorhombic (H42Q-1) and cubic (H42Q-2) modi®cations. The ®rst two were solved by ab initio direct methods using data collected to atomic resolution (1.20 and 0.93 A Ê , respectively). The recombinant wild type (rc-WT) with two HiPIP molecules in the asymmetric unit has 1264 protein atoms and 335 solvent sites, and is the second largest structure reported so far that has been solved by pure direct methods. The solutions were obtained in a fully automated way and included more than 80% of the protein atoms. Restrained anisotropic re®nement for rc-WT and H42Q-1 converged to R 1 jF o j À jF c j jF o j of 12.0 and 13.6%, respectively[data with I b 2'I], and 12.8 and 15.5% (all data). H42Q-2 contains two molecules in the asymmetric unit and diffracted only to 2.6 A Ê . In both molecules of rc-WT and in the single unique molecule of H42Q-1 the [Fe 4 S 4 ] 2+ cluster dimensions are very similar and show a characteristic tetragonal distortion with four short FeÐS bonds along four approximately parallel cube edges, and eight long FeÐS bonds. The unique protein molecules in H42Q-2 and rc-WT are also very similar in other respects, except for the hydrogen bonding around the mutated residue that is at the surface of the protein, supporting the hypothesis that the difference in redox potentials at lower pH values is caused primarily by differences in the charge distribution near the surface of the protein rather than by structural differences in the cluster region.

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Section: Assessment Of Standard Uncertaintiessupporting

confidence: 77%

Section: Cluster Geometrymentioning

confidence: 98%

Ab initio solution and refinement of two high-potential iron protein structures at atomic resolution

Parisini

Capozzi

Lubini

et al. 1999

Acta Crystallogr D Biol Cryst

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show abstract

“…The cluster structure is depicted in Fig. 2; selected interatomic distances are collected in (18)(19)(20)(21)(22)(23). The volumes in Table 2 were calculated from atomic coordinates (24) 6 , for which v CN ϭ 2,116 and 2,041 cm Ϫ1 , respectively.…”

Section: Resultsmentioning

confidence: 99%

Initial synthesis and structure of an all-ferrous analogue of the fully reduced [Fe ₄ S ₄ ] ⁰ cluster of the nitrogenase iron protein

Scott

Berlinguette²,

Holm³

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

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The synthetic cubane-type iron-sulfur clusters [Fe4S4(SR)4] z form a four-member electron transfer series (z ‫؍‬ 3؊, 2؊, 1؊, and 0), all members of which except that with z ‫؍‬ 0 have been isolated and characterized. (14). Evidence has been presented for a two-electron transfer by the fully reduced Fe protein in nitrogenase catalysis (15). Here, we demonstrate that the heretofore elusive all-ferrous state in a cubane-type cluster can be isolated in substance. Materials and Methods

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“…for C 72 H 52 Fe 2 S 4 : C,74.73;H,4.53;S,11.08. Found: C,74.72;H,4.51;S,11.09%. l eff (Evans method, 295 K): 4.2 l B .…”

Section: Synthesis Of [(Dpps)fe] 2 (L-sdpp) 2 (8)mentioning

confidence: 97%

“…for C 48 H 62 N 2 Fe 2 S 2 Si 4 : C, 60.36; H, 6.54;N,2.93;S,6.71. Found: C,59.90;H,6.05;N,2.85; S, 6.72%. l eff (Evans method, 296 K): 4.6 l B .…”

Section: Synthesis Of [{(Me 3 Si) 2 N}fe] 2 (L-sdpp) 2 (2)mentioning

confidence: 99%

Synthesis and characterization of heteroleptic iron(II) thiolate complexes with weak iron–arene interactions

Ohta

Ohki

Ikagawa

et al. 2007

Journal of Organometallic Chemistry

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Structural distortions of the [Fe4S4]2+ core of [Fe4S4(S-t-C4H9)4]2− in different crystalline environments and detection and instability of oxidized ([Fe4S4]3+) clusters

Cited by 58 publications

References 44 publications

Ab initio solution and refinement of two high-potential iron protein structures at atomic resolution

Ab initio solution and refinement of two high-potential iron protein structures at atomic resolution

Initial synthesis and structure of an all-ferrous analogue of the fully reduced [Fe ₄ S ₄ ] ⁰ cluster of the nitrogenase iron protein

Synthesis and characterization of heteroleptic iron(II) thiolate complexes with weak iron–arene interactions

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Structural distortions of the [Fe4S4]2+ core of [Fe4S4(S-t-C4H9)4]2− in different crystalline environments and detection and instability of oxidized ([Fe4S4]3+) clusters

Cited by 58 publications

References 44 publications

Ab initio solution and refinement of two high-potential iron protein structures at atomic resolution

Ab initio solution and refinement of two high-potential iron protein structures at atomic resolution

Initial synthesis and structure of an all-ferrous analogue of the fully reduced [Fe 4 S 4 ] 0 cluster of the nitrogenase iron protein

Synthesis and characterization of heteroleptic iron(II) thiolate complexes with weak iron–arene interactions

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Initial synthesis and structure of an all-ferrous analogue of the fully reduced [Fe ₄ S ₄ ] ⁰ cluster of the nitrogenase iron protein