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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]
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Metadata
- 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
- 33
- 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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › 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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