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Updated: Jan 29, 2026

Extraction of Cofactor F420 for Analysis of Polyglutamate Tail Length from Methanogenic Pure Cultures and Environmental Samples
Published on: October 14, 2021
New metal cofactors and recent metallocofactor insights
1Departments of Microbiology & Molecular Genetics and Biochemistry & Molecular Biology, Michigan State University, East Lansing, MI 48824, USA.
A novel nickel-pincer nucleotide (NPN) cofactor in lactate racemase is detailed. This review covers NPN
Area of Science:
- Biochemistry
- Bioinorganic Chemistry
- Enzymology
Background:
- Metalloenzymes utilize diverse metal cofactors at their active sites.
- Recent discovery of a nickel-pincer nucleotide (NPN) cofactor covalently linked to lactate racemase.
Purpose of the Study:
- To review the enzymatic function and biosynthesis of the NPN cofactor.
- To summarize recent advances in other organometallic and inorganic-cluster cofactors.
Main Methods:
- Literature review of recent advances in metalloenzyme cofactor research.
Main Results:
- Detailed description of the NPN cofactor in lactate racemase.
- Overview of lanthanide-pyrroloquinoline quinone, tungsten/molybdenum-pyranopterins, iron-guanylylpyridinol, nickel-tetrapyrrole F430, vanadium-iron cofactor, and nickel-iron-sulfur C-cluster functions.
- Summary of light-dependent changes in the manganese cluster of the oxygen-evolving complex.
Conclusions:
- The NPN cofactor represents a significant addition to known metalloenzyme cofactors.
- Diverse metal cofactors play crucial roles in various enzymatic processes, with ongoing research revealing new insights.
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