In vitro demetalation of central magnesium in various chlorophyll derivatives using Mg-dechelatase homolog from the chloroflexi Anaerolineae
Open accessAbstract
In the metabolic pathway of chlorophylls (Chls), an enzyme called STAY-GREEN or SGR catalyzes the removal of the central magnesium ion of Chls and their derivatives to their corresponding free bases, including pheophytins. The substrate specificity of SGR has been investigated through in vitro reactions using Chl-related molecules. However, information about the biochemical properties and reaction mechanisms of SGR and its substrate specificity remains elusive. In this study, we synthesized various Chl derivatives and investigated their in vitro dechelations using an SGR enzyme. Chl-a derivatives with the C3-vinyl group on the A-ring, which is commonly found as a substituent in natural substrates, and their analogs with ethyl, hydroxymethyl, formyl, and styryl groups at the C3-position were prepared as substrates. In vitro dechelatase reactions of these substrates were performed using an SGR enzyme derived from an Anaerolineae bacterium, allowing us to investigate their specificity. Reactivity was reduced for substrates with an electron-withdrawing formyl or sterically demanding styryl group at the C3-position. Furthermore, the Chl derivative with the C8-styryl group on the B-ring was less reactive for SGR dechelation than the C3-styryl substrate. These results indicate that the SGR enzyme recognizes substituents on the B-ring of substrates more than those on the A-ring.
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Homologues of Mg2+-dechelatase are present in some nonphotosynthetic Bacteria and Archaea but are lacking in cyanobacteria.
“Although homologues are present in some nonphotosynthetic Bacteria and Archaea,87,88 they are lacking in the cyanobacteria.”
From Metals in Motion: Understanding Labile Metal Pools in Bacteria (2025) · cites this paper as [88]
The Introduction (page not available in our copy) says SGR homologs occur in nonphotosynthetic bacteria and gives an Anaerolineae bacterium as an example. It does not address their presence in Archaea or their absence from cyanobacteria, so those parts of the claim are unsupported. (LLM, conf=0.86)
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Research works printed but not linked: 21
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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
- Authors
- Sato, S., Hirose, M., Tanaka, R., Ito, H., & Tamiaki, H.
- Affiliations
- Ritsumeikan University (JP)
- Hokkaido University (JP)
- Corresponding author
- Tamiaki, Hitoshi
- Venue
- Photosynthesis Research
- Published
- 2024-03-26
- Volume
- 160
- Issue
- 1
- Pages
- 45-53
- ISSN
- 0166-8595 (ISSN-L)
- 1573-5079
- PMC
- PMC11006732
- OpenAlex
- W4393196340
- Cited by
- 8
- References
- 0
- Citations by year
- 2026: 3 · 2025: 2 · 2024: 3
- FWCI
- 0.78
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Locations
- Photosynthesis Research (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Japan Society for the Promotion of Science (21J22995, 23H04960, 23K0569103, 22H02203)
- Ritsumeikan University
- Topics
- Physical Sciences › Materials Science › Materials Chemistry › Porphyrin and Phthalocyanine Chemistry
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Photosynthetic Processes and Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Porphyrin Metabolism and Disorders
- Keywords
- stay-green, chlorophyll derivatives, pheophytin, substrate specificity, chlorophyll biosynthesis, Anaerolineae, Chloroflexi, enzyme mechanism
- MeSH terms
- Chlorophyll, Enzymes, Magnesium, Pheophytins, Chloroflexi
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