Structural and catalytic chemistry of magnesium-dependent enzymes
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Ribosomes and other negatively charged macromolecules and metabolites buffer free Mg2+ near 1 mM, with a range of ~0.3 to 3 mM.
“Collectively, ribosomes and other negatively charged macromolecules and metabolites buffer free Mg2+ near 1 mM, with a range of ∼0.3 to 3 mM.5,8,71,72”
From Metals in Motion: Understanding Labile Metal Pools in Bacteria (2025) · cites this paper as [71]
A subset of Mg2+-dependent enzymes form relatively stable associations with Mg2+ (Kd of 10-100 μM).
“Although many Mg2+-dependent enzymes bind to ATP:Mg2+ (or other substrate:Mg2+ complexes), a subset form relatively stable associations with Mg2+ (Kd of 10–100 μM),71 and it is possible that some of this Mg2+ may be functionally sequestered.”
From Metals in Motion: Understanding Labile Metal Pools in Bacteria (2025) · cites this paper as [71]
Cited by
Sorted by citations
Small-Molecule Two-Photon Probes for Bioimaging Applications
Kim, H. M., & Cho, B. R. (2015) · Chemical Reviews · doi:10.1021/cr5004425 · Cited by 1,047 · see citing works
Metals in Motion: Understanding Labile Metal Pools in Bacteria
Helmann, J. D. (2025) · Biochemistry · doi:10.1021/acs.biochem.4c00726 · Cited by 49 · see citing works
Diverse relationships between metal ions and the ribosome
Akanuma, G. (2021) · Bioscience, Biotechnology, and Biochemistry · doi:10.1093/bbb/zbab070 · Cited by 34 · see citing works
Akanuma, G., Yamazaki, K., Yagishi, Y., Iizuka, Y., Ishizuka, M., Kawamura, F., & Kato-Yamada, Y. (2018) · Journal of Bacteriology · doi:10.1128/jb.00212-18 · Cited by 27 · see citing works
- Authors
- Cowan, J. A.
- Affiliations
- The Ohio State University (US)
- Corresponding author
- Cowan, J.A.
- ORCID
- Cowan, J.A.
- Venue
- Biometals
- Published
- 2002-09
- Volume
- 15
- Issue
- 3
- Pages
- 225-235
- ISSN
- 0966-0844 (ISSN-L)
- 1572-8773
- OpenAlex
- W1537110470
- Cited by
- 428
- References
- 0
- Citations by year
- 2026: 25 · 2025: 34 · 2024: 23 · 2023: 24 · 2022: 25 · 2021: 22 · 2020: 28 · 2019: 17 · 2018: 36 · 2017: 20 · 2016: 14 · 2015: 25 · 2014: 26 · 2013: 16 · 2012: 25
- FWCI
- 0.27
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- Locations
- BioMetals (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Keywords
- magnesium-dependent enzyme, enzyme structure, enzyme catalysis, metalloenzymes, magnesium ions, enzyme active site
- MeSH terms
- Catalysis, Enzymes, Magnesium, Nucleic Acids, Phosphorylation, Molecular Structure
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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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