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Query: KEGG:D04166 (FeCl3)
 1,389 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

ATP-Fe and AMP-Fe complexes in water (H2O and 2H2O) at pH 7.5 were studied using Raman spectroscopy. Parallel and perpendicular polarization spectra were recorded in the spectral range 200-1650 cm-1, and the depolarization ratios for most of the bands were calculated. The changes in the frequencies, intensities and depolarization ratios of the ATP and AMP bands after the addition of FeCl3 showed that the adenine moiety, in addition to the phosphate(s), was involved in the binding of Fe to both ATP and AMP. Direct interactions of Fe(III) with the phosphate chain and the N-7 nitrogen and indirect interaction (via water molecules) with the amide group were proposed for the ATP-Fe complex. In contrast, direct interaction with the phosphate group and indirect interaction with the amide group were observed for the AMP-Fe complex. The different interactions of the two complexes suggest an 'anti' conformation for the ATP-Fe complex and a 'syn' conformation for the AMP-Fe complex. The strong binding of Fe to ATP compared with AMP and the difference in the conformation of the ATP-Fe and the AMP-Fe complexes may be significant in the pathway of Fe release in mitochondria.
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PMID:A Raman study of the binding of Fe(III) to ATP and AMP. 144 15

Acetyl-CoA synthetase was purified 800-fold from Bradyrhizobium japonicum bacteroids. A specific activity of 16 mumol/min per mg of protein was achieved, with a 30-40% yield. The purification scheme consisted of only three consecutive chromatography steps. The enzyme has a native Mr of 150,000, estimated by gel-permeation chromatography, and a subunit Mr of 72,000, determined by SDS/polyacrylamide-gel electrophoresis. The optimum pH and temperature are 8.5 and 50 degrees C respectively. The Km values for acetate, CoA and ATP were 146, 202 and 275 microM respectively. The reaction was specific for acetate, as propionate and oleate were used very poorly. Likewise, the enzyme used only ATP, ADP or dATP; AMP, GTP, XTP and UTP could not replace ATP. Acetyl-CoA synthetase showed a broad specificity for metals; MnCl2 could replace MgCl2. In addition, CaCl2 and CoCl2 were approx. 50% as effective as MgCl2, but FeCl3, NiCl2 or ZnCl2 could not effectively substitute for MgCl2. The enzyme may be regulated by NADP+ and pyruvate; no effect was seen of amino acids, glucose catabolites, reduced nicotinamide nucleotides or acetyl-CoA. Inhibition was seen with AMP, PPi, FMN and pyridoxal phosphate, with Ki values of 720, 222, 397 and 1050 microM respectively.
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PMID:Purification and properties of acetyl-CoA synthetase from Bradyrhizobium japonicum bacteroids. 197 Feb 39

Our earlier studies showed that rabbit muscle phosphoglucomutase was irreversibly inactivated by exposure to a mixture of vitamin C, FeCl3 and O2. The enzyme lost about 70% of its phosphate (V.V. Desphande and J.G. Joshi, J. Biol. Chem. 260, 754-764, 1985). The present report shows that several other iron proteins can substitute for FeCl3 to a varying degree. The rate of inactivation by FeCl3 greater than ferritin greater than hemoglobin = hemerythrin greater than transferrin = ferridoxin = vitamin C. These iron compounds also produced dephosphoenzyme but did not dephosphorylate ATP, ADP, AMP or phospholipids.
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PMID:Differential loss of enzyme activity by vitC and iron containing proteins. 295 84