Iron-sulfur proteins: Recent developments in the field (original) (raw)
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The binding of amino acids to the differentiated iron in 3:1 site-differentiated {Fe4S4} clusters
Inorganica Chimica Acta, 1997
The 3:l site-differentiated clusters [PPh&(Fe$,(L)(SEt)] (1.2) and [NE&],[Fe,S,(L)(SEt)] (3.4) (L-L' or L*; H$.'= 1.4,7tris(4-sulfanylbenzoyl)-1A.7-triazacyclononanene. HsL 2 -1.5.9-tris(esulfany1benzoyl)-l~,9-ui molar amounts of amino acid methyl ester in dimethyl sulfoxide solution form the amino [Fe.&(L) ( AA-OMe) 12-( HAA-OMe = HCys-OMe. L-cysteine methyl ester (5-8); HTyr-0 OMe. DL-serine methyl ester ( 17-20)) or [Fe&(L) ( HHis-OMe) ] -( HHis-OMe equiv. of HCys-OMe were employed in the. reaction cysteinato-bridged dhnetic (Feds were prepared. Clusters 5-22 have been characterised by 'H NMR, M6ssbauer and coordinated by ligand (L) and amino acid ester, at the fourth, differentiated iron site, i in some metalloproteins. including the nitrogenase iron-molybdenum cofactor and P-clusters and the distal (Fe&) clu hydrogenase of Desulfovibrio gigas.
Insights into properties and energetics of iron–sulfur proteins from simple clusters to nitrogenase
Current Opinion in Chemical Biology, 2002
AF antiferromagnetic BS broken symmetry DFT density functional theory ENDOR electron-nuclear double resonance Fd ferredoxin HIPIP high-potential iron-sulfur protein HS high-spin LUMO lowest unoccupied molecular orbital PDR phthalate dioxygenase reductase RPBE revised Perdew-Burke-Enzerhoff SCF self-consistent-field Uncoupled state Heisenberg Broken symmetry 9J J (25/2)J (5/2)J Current Opinion in Chemical Biology
THE COMPETITION BETWEEN CHEMISTRY AND BIOLOGY IN ASSEMBLING IRON–SULFUR DERIVATIVES. MOLECULAR STRUCTURES AND ELECTROCHEMISTRY. PART III. {Fe2S23(X)} (X = Asp, Arg, His) and {Fe2S22(His)2} PROTEINS
Coordination Chemistry Reviews, 2016
Iron-sulfur clusters are ubiquitous and evolutionary ancient prosthetic groups which participate in crucial electron transfer processes. Just in view of such a significant aspect we planned to update their structure and electrochemistry. In this picture, after having reviewed {Fe(Cys)4} rubredoxins (Coord. Chem. Rev., 257 (2013) 1777-1805) and {[Fe2S2](Cys)4} ferredoxins (Coord. Chem. Rev., 280 (2103) 50-83), we will now deal with Rieske proteins (which have {[Fe2S2](Cys)2(His)2} clusters as redox active centre), also discussing about proteins having {[Fe2S2](Cys)3(X)} (X = Asp, Arg, His) redox active centres, which can be considered as intermediates between classical {[Fe2S2](Cys)4} (hereafter [2Fe-2S]) and Rieske proteins (hereafter [2Fe-2S]R). As usual, we will also deal with the synthetic analogues of the iron-sulfur clusters of Rieske proteins.
Journal of Biological Chemistry, 2011
Succinate-ubiquinone oxidoreductase (SQR) and menaquinol-fumarate oxidoreductase (QFR) from Escherichia coli are members of the complex II family of enzymes. SQR and QFR catalyze similar reactions with quinones; however, SQR preferentially reacts with higher potential ubiquinones, and QFR preferentially reacts with lower potential naphthoquinones. Both enzymes have a single functional quinone-binding site proximal to a [3Fe-4S] iron-sulfur cluster. A difference between SQR and QFR is that the redox potential of the [3Fe-4S] cluster in SQR is 140 mV higher than that found in QFR. This may reflect the character of the different quinones with which the two enzymes preferentially react. To investigate how the environment around the [3Fe-4S] cluster affects its redox properties and catalysis with quinones, a conserved amino acid proximal to the cluster was mutated in both enzymes. It was found that substitution of SdhB His-207 by threonine (as found in QFR) resulted in a 70-mV lowering of the redox potential of the cluster as measured by EPR. The converse substitution in QFR raised the redox potential of the cluster. X-ray structural analysis suggests that placing a charged residue near the [3Fe-4S] cluster is a primary reason for the alteration in redox potential with the hydrogen bonding environment having a lesser effect. Steady state enzyme kinetic characterization of the mutant enzymes shows that the redox properties of the [3Fe-4S] cluster have only a minor effect on catalysis.
1993
Ferredoxin from Methanosarcina thermophila is an electron acceptor for the CO dehydrogenase complex which decarbonylates acetyl-coenzyme A and oxidizes the carbonyl group to carbon dioxide in the pathway for conversion of the methyl group of acetate to methane (K. C. Terlesky and J. G. Ferry, J. Biol. Chem. 263:4080-4082, 1988). Resonance Raman spectroscopy and electron paramagnetic resonance spectroelectro-chemistry indicated that the ferredoxin contained two [4Fe-4S] clusters per monomer of 6,790 Da, each with a midpoint potential of- 407 mV. A [3Fe-4S] species, with a midpoint potential of + 103 mV, was also detected in the protein at high redox potentials. Quantitation of the [3Fe-4S] and [4Fe-4S] centers revealed 0.4 and 2.1 spins per monomer, respectively. The iron-sulfur clusters were unstable in the presence of air, and the rate of cluster loss increased with increasing temperature. A ferredoxin preparation, with a low spin quantitation of [4Fe-4S] centers, was treated with ...
Evidence for reversible multiple redox transformations of [3Fe-4S] clusters
FEBS Letters, 1989
Analysis of the diffusionless cyclic voltammetry of ferredoxin III from Desulfovibrio africanus, co-adsorbed with neomycin as an electroactive film on pyrolytic graphite 'edge' electrodes, shows that the reduced [3Fe-4S]@) cluster undergoes further fast, chemically reversible, two-electron reduction, at a potential I?" =ca. -720 mV (pH 7.15, 0°C). The pH dependence of l?' @H 6.25-7.80) indicates net transfer of two H+. Observation of similar voltammetric waves in other proteins specifically containing [3Fe-4S] centres suggests that extensive redox activity and stabilisation of what is formally an all-Fe(I1) species, may be a common, perhaps characteristic, feature of this cluster type. Ferredoxin; Iron-sulphur; Electron transfer; Voltammetry; Electrochemistry; (Desulfovibrio africanus) Published by Elsevier Science Publishers B. V. (Biomedical Division) 00145793/89/$3.50 0 1989 Federation of European Biochemical Societies
Spontaneous assembly of redox-active iron-sulfur clusters at low concentrations of cysteine
Nature Communications, 2021
Iron-sulfur (FeS) proteins are ancient and fundamental to life, being involved in electron transfer and CO2 fixation. FeS clusters have structures similar to the unit-cell of FeS minerals such as greigite, found in hydrothermal systems linked with the origin of life. However, the prebiotic pathway from mineral surfaces to biological clusters is unknown. Here we show that FeS clusters form spontaneously through interactions of inorganic Fe2+/Fe3+ and S2− with micromolar concentrations of the amino acid cysteine in water at alkaline pH. Bicarbonate ions stabilize the clusters and even promote cluster formation alone at concentrations >10 mM, probably through salting-out effects. We demonstrate robust, concentration-dependent formation of [4Fe4S], [2Fe2S] and mononuclear iron clusters using UV-Vis spectroscopy, 57Fe-Mössbauer spectroscopy and 1H-NMR. Cyclic voltammetry shows that the clusters are redox-active. Our findings reveal that the structures responsible for biological electr...
Selective oxidative destruction of iron-sulfur clusters
FEBS Letters, 1985
The destructive oxidation of aerobically isolated 7Fe Azotobacter vinelandii ferredoxin I [(7Fe)FdI] by Fe(CN)",-is examined using low-temperature magnetic circular dichroism (MCD) and EPR. The results demonstrate that oxidation of the [3Fe-3S] cluster occurs only after essentially complete destruction of the [4Fe-4S] cluster. It is therefore feasible by controlled Fe(CN);-oxidation to obtain a partially metallated form of FdI, (3Fe)FdI, containing only a [3Fe-3s) cluster. The MCD and EPR data demonstrate that the [3Fe-3S] cluster in (3Fe)FdI is essentially identical in structure to that in the native protein.