Glycine reductase mechanism
Abstract
The ability of some anaerobic bacteria to conserve energy via a soluble substrate level phosphorylation system by reducing glycine to acetyl-phosphate has been an intriguing mechanism for about half a century. The genes implicated in this system have been sequenced and form an operon structure with those of the thioredoxin system. The deduced proteins exhibit high degrees of similarity with glycine reductase from other bacteria. Faster progress in understanding the exact mechanisms is hampered, for example, by some unique reactions involving selenoethers and redox active selenocysteines, which do not allow an easy heterologous formation in Escherichia coli. Further major obstacles are the processing of a substrate-specific pro-protein to a new carbonyl/pyruvoyl group in one of the two peptides formed that stabilize the substrate-binding selenoprotein, which contains an additional rather unstable carbonyl group.
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Reductive SLP takes place via acetyl phosphate synthesis at the glycine reductase reaction and subsequent phosphorylation of ADP.
“Reductive SLP also takes place via acetyl phosphate synthesis at the glycine reductase reaction (Andreesen, 2004) and the subsequent phosphorylation of ADP.”
From Serpentinization as the source of energy, electrons, organics, catalysts, nutrients and pH gradients for the origin of LUCA and life (2023) · cites this paper as Andreesen, 2004
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- Authors
- Andreesen, J. R.
- Affiliations
- Martin Luther University Halle-Wittenberg (DE)
- Corresponding author
- Andreesen, Jan R
- Venue
- Current Opinion in Chemical Biology
- Publisher
- Elsevier BV
- Published
- 2004-10
- Volume
- 8
- Issue
- 5
- Pages
- 454-461
- ISSN
- 1367-5931 (ISSN-L)
- OpenAlex
- W2016519332
- Cited by
- 86
- References
- 44
- Citations by year
- 2026: 4 · 2025: 7 · 2024: 11 · 2023: 12 · 2022: 2 · 2021: 2 · 2020: 5 · 2019: 7 · 2018: 4 · 2016: 4 · 2015: 2 · 2014: 5 · 2012: 4
- FWCI
- 0.28
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Current Opinion in Chemical Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Grains Research and Development Corporation
- Deutsche Forschungsgemeinschaft
- Topics
- Health Sciences › Nursing › Nutrition and Dietetics › Selenium in Biological Systems
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Toxicology › Organoselenium and organotellurium chemistry
- Keywords
- glycine reductase, anaerobic bacteria, substrate-level phosphorylation, thioredoxin system, selenocysteine, selenoethers, selenoproteins, enzyme mechanism, gene operon
- MeSH terms
- Amino Acid Oxidoreductases, Binding Sites, Escherichia coli, Multienzyme Complexes, Operon, Oxidation-Reduction, Proteins, Receptors, Fc, Staphylococcal Protein A, Thioredoxin-Disulfide Reductase, Selenoproteins
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