Fluorination of a conserved tyrosine in POR offers new clues for proton transfer
© 2024 Federation of European Biochemical Societies..
Reduction of the 17,18-double bond in the D-ring during chlorophyll biosynthesis is catalyzed by the rare, naturally occurring photoenzyme protochlorophyllide oxidoreductase (POR). A conserved tyrosine residue has been suggested to donate a proton to C18 of the substrate in the past decades. Taylor and colleagues scrutinized the model with a powerful tool that utilized a modified genetic code to introduce fluorinated tyrosine analogues into POR. The presented results show that the suggested catalytically critical tyrosine is unlikely to participate in the reaction chemistry but is required for substrate binding, and instead, a cysteine residue preceding the lid helix is proposed to have the role of proton donor.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2024 |
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| Erschienen: |
2024 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:291 |
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| Enthalten in: |
The FEBS journal - 291(2024), 7 vom: 29. Apr., Seite 1400-1403 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Dong, Chen-Song [VerfasserIn] |
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| Links: |
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| Anmerkungen: |
Date Completed 04.04.2024 Date Revised 16.04.2024 published: Print-Electronic Citation Status MEDLINE |
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| doi: |
10.1111/febs.17074 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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NLM367872587 |
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| 520 | |a Reduction of the 17,18-double bond in the D-ring during chlorophyll biosynthesis is catalyzed by the rare, naturally occurring photoenzyme protochlorophyllide oxidoreductase (POR). A conserved tyrosine residue has been suggested to donate a proton to C18 of the substrate in the past decades. Taylor and colleagues scrutinized the model with a powerful tool that utilized a modified genetic code to introduce fluorinated tyrosine analogues into POR. The presented results show that the suggested catalytically critical tyrosine is unlikely to participate in the reaction chemistry but is required for substrate binding, and instead, a cysteine residue preceding the lid helix is proposed to have the role of proton donor | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a chlorophyll biosynthesis | |
| 650 | 4 | |a enzyme mechanism | |
| 650 | 4 | |a non‐canonical amino acid | |
| 650 | 4 | |a photocatalysis | |
| 650 | 7 | |a Oxidoreductases Acting on CH-CH Group Donors |2 NLM | |
| 650 | 7 | |a EC 1.3.- |2 NLM | |
| 650 | 7 | |a Protochlorophyllide |2 NLM | |
| 650 | 7 | |a 20369-67-9 |2 NLM | |
| 650 | 7 | |a Protons |2 NLM | |
| 650 | 7 | |a protochlorophyllide reductase |2 NLM | |
| 650 | 7 | |a EC 1.3.1.33 |2 NLM | |
| 650 | 7 | |a Chlorophyll |2 NLM | |
| 650 | 7 | |a 1406-65-1 |2 NLM | |
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