Binding of the competitive inhibitor dCDP to ribonucleoside-diphosphate reductase from Escherichia coli studied by 1H NMR. Different properties of the large protein subunit and the holoenzyme.
作者： Peter ALLARD , Sergei KUPRIN , Binghua SHEN , Anders EHRENBERG
DOI: 10.1111/J.1432-1033.1992.TB17229.X
关键词: Binding constant 、 Protein subunit 、 Ribonucleotide reductase 、 Binding site 、 Nuclear magnetic resonance spectroscopy 、 Reductase 、 Chemistry 、 Plasma protein binding 、 Stereochemistry 、 Peptide
摘要: Ribonucleoside-diphosphate reductase (EC 1.17.4.1) from Escherichia coli consists of two nonidentical subunits, proteins R1 and R2. The binding the product dCDP to protein holoenzyme R1R2 has been studied by means 1H-NMR spectroscopy. In presence effector dTTP at 25 degrees C, was found be in rapid exchange between sites solvent which results a broadening resonances. When both R2 are present, so that complex is formed, smaller observed than with alone. No further linewidth decrease when [R2]/[R1] ratio exceeded 1. constant or same, Kd = 0.9 mM. resonances as compared may explained combination effects: (a) overall tumbling time will increase going R1R2, cause correspondingly, (b) twofold number exchange, factor 0.5. effect without iron (apoR2) reduced native R2, probably because some denatured proteins, while C-terminal peptide did not any narrowing all.
sci-hub.se 参考文章(31)
Curtis L. Atkin, Lars Thelander, Peter Reichard, George Lang, Iron and Free Radical in Ribonucleotide Reductase EXCHANGE OF IRON AND MÖSSBAUER SPECTROSCOPY OF THE PROTEIN B2 SUBUNIT OF THE ESCHERICHIA COLI ENZYME Journal of Biological Chemistry. ,vol. 248, pp. 7464- 7472 ,(1973) , 10.1016/S0021-9258(19)43313-9
Lars Thelander, Britt-Marie Sjöberg, Staffan Eriksson, [30] Ribonucleoside diphosphate reductase (Escherichia coli) Methods in Enzymology. ,vol. 51, pp. 227- 237 ,(1978) , 10.1016/S0076-6879(78)51032-X
Harvey S. Penefsky, [47] A centrifuged-column procedure for the measurement of ligand binding by beef heart F1 Methods in Enzymology. ,vol. 56, pp. 527- 530 ,(1979) , 10.1016/0076-6879(79)56050-9
U von Döbeln, P Reichard, Binding of substrates to Escherichia coli ribonucleotide reductase. Journal of Biological Chemistry. ,vol. 251, pp. 3616- 3622 ,(1976) , 10.1016/S0021-9258(17)33389-6
Lars Thelander, Physicochemical Characterization of Ribonucleoside Diphosphate Reductase from Escherichia coli Journal of Biological Chemistry. ,vol. 248, pp. 4591- 4601 ,(1973) , 10.1016/S0021-9258(19)43705-8
The iron center in ribonucleotide reductase from Escherichia coli. Journal of Biological Chemistry. ,vol. 255, pp. 6706- 6712 ,(1980) , 10.1016/S0021-9258(18)43628-9
M Fontecave, R Eliasson, P Reichard, Enzymatic regulation of the radical content of the small subunit of Escherichia coli ribonucleotide reductase involving reduction of its redox centers. Journal of Biological Chemistry. ,vol. 264, pp. 9164- 9170 ,(1989) , 10.1016/S0021-9258(18)60509-5
N P Morris, D R Keene, R W Glanville, H Bentz, R E Burgeson, The tissue form of type VII collagen is an antiparallel dimer. Journal of Biological Chemistry. ,vol. 261, pp. 5638- 5644 ,(1986) , 10.1016/S0021-9258(19)57262-3
A Larsson, M Karlsson, M Sahlin, B M Sjöberg, Radical formation in the dimeric small subunit of ribonucleotide reductase requires only one tyrosine 122. Journal of Biological Chemistry. ,vol. 263, pp. 17780- 17784 ,(1988) , 10.1016/S0021-9258(19)77903-4
Peter Reichard, Enzymatic synthesis of deoxyribonucleotides. I. Formation of deoxycytidine diphosphate from cytidine diphosphate with enzymes from Escherichia coli. Journal of Biological Chemistry. ,vol. 237, pp. 3513- 3519 ,(1962) , 10.1016/S0021-9258(19)70849-7