Three-iron clusters in iron-sulfur proteins.
Contents. 1. Introduction and history. 2. Characteristic spectroscopic features of 3Fe clusters. 1. General considerations. 2. Mössbauer spectroscopy. 3. Magnetic circular dichroism (MCD) spectroscopy. 4. Electron paramagnetic resonance (EPR) spectroscopy. 5. Resonance Raman (RR) spectroscopy. 6. Extended X-ray fine-structure (EXAFS) spectroscopy. 3. Results of X-Ray diffraction studies. 4. Proteins containing or showing features characteristic of 3Fe clusters 1. Overview. 2. Ferredoxin I of Azotobacter vinelandii. 3. Ferredoxin II of Desulfovibrio gigas. 4. Aconitase from beef heart. 5. Other observations and considerations relevant to 3Fe clusters or cluster interconversions 1. Oxidative degradation of [4Fe-4S] clusters to 3Fe clusters. 2. Extrusion studies on 3Fe clusters. 3. Reconstitution of 3Fe clusters. 4. Disposition of iron ligands in cluster interconversions. 6. Do all 3Fe clusters have the same structure? Evidence for [3Fe-4S] clusters. 7. Are 3Fe clusters artifacts or biologically significant structures?
D000154:Aconitate Hydratase / Q000032:analysis; D000818:Animals; D001426:Bacterial Proteins / Q000032:analysis; D002417:Cattle; D055598:Chemical Phenomena; D002621:Chemistry; D007501:Iron; D007506:Iron-Sulfur Proteins; D008667:Metalloproteins; D009206:Myocardium / Q000201:enzymology; D010084:Oxidation-Reduction; D013045:Species Specificity; D013057:Spectrum Analysis / Q000379:methods; D013329:Structure-Activity Relationship
D001426:Bacterial Proteins; D007506:Iron-Sulfur Proteins; D008667:Metalloproteins; D007501:Iron; D000154:Aconitate Hydratase