Structural and catalytic chemistry of magnesium-dependent enzymes

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Binuclear Metallohydrolases

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STRUCTURES OF TERNARY COMPLEXES OF RAT DNA POLYMERASE BETA, A DNA TEMPLATE-PRIMER, AND DDCTP

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Metal Activation of Enzymes in Nucleic Acid Biochemistry

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Recognition and Cleavage of DNA by Type‐II Restriction Endonucleases

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Novel subunit—subunit interactions in the structure of glutamine synthetase

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The Biological chemistry of magnesium

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A helical arch allowing single-stranded DNA to thread through T5 5'-exonuclease

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Structure of Bacteriophage T4 RNase H, a 5′ to 3′ RNA–DNA and DNA–DNA Exonuclease with Sequence Similarity to the RAD2 Family of Eukaryotic Proteins

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Refined atomic model of glutamine synthetase at 3.5 Å resolution

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Free energy relationships in metalloenzyme-catalyzed reactions. Calculations of the effects of metal ion substitutions in staphylococcal nuclease

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Structural model for the reaction mechanism of glutamine synthetase, based on five crystal structures of enzyme-substrate complexes

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Divalent Metal Ions at the Active Sites of the EcoRV and EcoRI Restriction Endonucleases

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Biological coordination chemistry of magnesium, sodium, and potassium ions. Protein and nucleotide binding sites

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Substrate-assisted catalysis in the cleavage of DNA by the EcoRI and EcoRV restriction enzymes.

Jeltsch, A., Alves, J., Wolfes, H., Maass, G., & Pingoud, A. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.18.8499 · Cited by 116

The crystal structure and active site location of isocitrate lyase from the fungus Aspergillus nidulans

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Rapid Reaction Analysis of the Catalytic Cycle of the EcoRV Restriction Endonuclease

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On the catalytic mechanism of EcoRI and EcoRV A detailed proposal based on biochemical results, structural data and molecular modelling

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Metallobiochemistry of magnesium. Coordination complexes with biological substrates: site specificity, kinetics and thermodynamics of binding, and implications for activity

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Mutagenic investigation of conserved functional amino acids in Escherichia coli L-aspartase.

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Metal ion-assisted stacking interactions and the facilitated hydrolysis of nucleoside 5 ¢ -triphosphates

Sigel, H. (1998) · Pure and Applied Chemistry · doi:10.1351/pac199870040969 · Cited by 41

Inert Chromium and Cobalt Complexes as Probes of Magnesium‐Dependent Enzymes

Black, C. B., & Cowan, J. A. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.00684.x · Cited by 27

A critical evaluation of metal-promoted Klenow 3′-5′ exonuclease activity: calorimetric and kinetic analyses support a one-metal-ion mechanism

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Magnesium activation of nuclease enzymes—the importance of water

Cowan, J. A. (1998) · Inorganica Chimica Acta · doi:10.1016/s0020-1693(98)00073-5 · Cited by 25

Wild-type and mutant d -xylose isomerase from Actinoplanes missouriensis: metal-ion dissociation constants, kinetic parameters of deuterated and non-deuterated substrates and solvent-isotope effects

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Magnesium νs. manganese cofactors for metallonuclease enzymes. A critical evaluation of thermodynamic binding parameters and stoichiometry

Casareno, R. L. B., & Cowan, J. A. (1996) · Chemical Communications · doi:10.1039/cc9960001813 · Cited by 24

Mechanism-Based Inactivation of L-Aspartase from Escherichia coli

Schindler, J. F., & Viola, R. E. (1994) · Biochemistry · doi:10.1021/bi00197a042 · Cited by 12

Mechanism of metal-promoted catalysis of nucleic acid hydrolysis by Escherichia coli ribonuclease H

Black, C. B., Foster, M. P., & Cowan, J. A. (1996) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s007750050084 · Cited by 11

ChemInform Abstract: Metal‐Assisted Stacking Interactions and the Facilitated Hydrolysis of Nucleoside 5′‐Triphosphates

Sigel, H. (1999) · ChemInform · doi:10.1002/chin.199901302 · Cited by 1

Small-Molecule Two-Photon Probes for Bioimaging Applications

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Nucleases: diversity of structure, function and mechanism

Yang, W. (2011) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583510000181 · Cited by 692

Magnesium deficiency in plants: An urgent problem

Guo, W., Nazim, H., Liang, Z., & Yang, D. (2015) · The Crop Journal · doi:10.1016/j.cj.2015.11.003 · Cited by 605

Second messenger role for Mg2+ revealed by human T-cell immunodeficiency

Li, F.-Y., Chaigne-Delalande, B., Kanellopoulou, C., Davis, J. C., Matthews, H. F., Douek, D. C., Cohen, J. I., Uzel, G., Su, H. C., & Lenardo, M. J. (2011) · Nature · doi:10.1038/nature10246 · Cited by 579

Turning main-group element magnesium into a highly active electrocatalyst for oxygen reduction reaction

Liu, S., Li, Z., Wang, C., Tao, W., Huang, M., Zuo, M., Yang, Y., Kang, Y., Zhang, L., Chen, S., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-14565-w · Cited by 438

Structural and catalytic roles for divalent magnesium in nucleic acid biochemistry

Sreedhara, A., & Cowan, J. A. (2002) · BioMetals · doi:10.1023/a:1016070614042 · Cited by 90

The inhibition of Mg (II)-enolase by other activating metal ions

Malmström, B. G. (1961) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(61)90180-9 · Cited by 3

Magnesium chemistry and biochemistry

Maguire, M. E., & Cowan, J. A. (2002) · BioMetals · doi:10.1023/a:1016058229972 · Cited by 614

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Verbindungen des einwertigen Magnesiums als Polymerisationskatalysatoren

Stroh, R., & Nützel, K. (1960) · Angewandte Chemie · doi:10.1002/ange.19600722415