Vitamin B12 model complex catalyzed methyl transfer reaction to alkylthiol under electrochemical conditions with sacrificial electrode

2009 ◽  
pp. 9898 ◽  
Author(s):  
Ling Pan ◽  
Hisashi Shimakoshi ◽  
Takahiro Masuko ◽  
Yoshio Hisaeda
Keyword(s):  
Vitamin B12 ◽  
Transfer Reaction ◽  
Methyl Transfer ◽  
Model Complex

Methyl-transfer reaction to alkylthiol catalyzed by a simple vitamin B12 model complex using zinc powder

2011 ◽  
Vol 368 (1) ◽  
pp. 194-199 ◽  
Author(s):  
Ling Pan ◽  
Keishiro Tahara ◽  
Takahiro Masuko ◽  
Yoshio Hisaeda
Keyword(s):  
Vitamin B12 ◽  
Transfer Reaction ◽  
Zinc Powder ◽  
Methyl Transfer ◽  
Model Complex

Electrochemical Methyl-transfer Reaction to Alkylthiol Catalyzed by Hydrophobic Vitamin B12

2009 ◽  
Vol 38 (1) ◽  
pp. 26-27 ◽  
Author(s):  
Ling Pan ◽  
Hisashi Shimakoshi ◽  
Yoshio Hisaeda
Keyword(s):  
Vitamin B12 ◽  
Transfer Reaction ◽  
Methyl Transfer

scholarly journals The thiostrepton A tryptophan methyltransferase TsrM catalyses a cob(II)alamin-dependent methyl transfer reaction

2015 ◽  
Vol 6 (1) ◽  
Author(s):  
Alhosna Benjdia ◽  
Stéphane Pierre ◽  
Carmen Gherasim ◽  
Alain Guillot ◽  
Manon Carmona ◽  
...  
Keyword(s):  
Transfer Reaction ◽  
Methyl Transfer

Methyl transfer from a hydrophobic vitamin B12 derivative to arsenic trioxide

2009 ◽  
Vol 694 (6) ◽  
pp. 916-921 ◽  
Author(s):  
Koichiro Nakamura ◽  
Yoshio Hisaeda ◽  
Ling Pan ◽  
Hiroshi Yamauchi
Keyword(s):  
Vitamin B12 ◽  
Arsenic Trioxide ◽  
Methyl Transfer

Synthesis, characterization, Co–S bond reactivity of a vitamin B12 model complex having pentafluorophenylthiolate as an axial ligand

2013 ◽  
Vol 42 (18) ◽  
pp. 6410 ◽  
Author(s):  
Keishiro Tahara ◽  
Ayaka Matsuzaki ◽  
Takahiro Masuko ◽  
Jun-ichi Kikuchi ◽  
Yoshio Hisaeda
Keyword(s):  
Vitamin B12 ◽  
Axial Ligand ◽  
Model Complex

scholarly journals Flagellin lysine methyltransferase FliB catalyzes a [4Fe-4S] mediated methyl transfer reaction

2021 ◽  
Vol 17 (11) ◽  
pp. e1010052
Author(s):  
Chu Wang ◽  
Christian Nehls ◽  
Dirk Baabe ◽  
Olaf Burghaus ◽  
Robert Hurwitz ◽  
...  
Keyword(s):  
Transfer Reaction ◽  
Radical Mechanism ◽  
Zero Field ◽  
Paramagnetic Resonance ◽  
Methyl Transfer ◽  
Lysine Residues ◽  
Oxygen Sensitive ◽  
Flagellar Filament

The methyltransferase FliB posttranslationally modifies surface-exposed ɛ-N-lysine residues of flagellin, the protomer of the flagellar filament in Salmonella enterica (S. enterica). Flagellin methylation, reported originally in 1959, was recently shown to enhance host cell adhesion and invasion by increasing the flagellar hydrophobicity. The role of FliB in this process, however, remained enigmatic. In this study, we investigated the properties and mechanisms of FliB from S. enterica in vivo and in vitro. We show that FliB is an S-adenosylmethionine (SAM) dependent methyltransferase, forming a membrane associated oligomer that modifies flagellin in the bacterial cytosol. Using X-band electron paramagnetic resonance (EPR) spectroscopy, zero-field 57Fe Mössbauer spectroscopy, methylation assays and chromatography coupled mass spectrometry (MS) analysis, we further found that FliB contains an oxygen sensitive [4Fe-4S] cluster that is essential for the methyl transfer reaction and might mediate a radical mechanism. Our data indicate that the [4Fe-4S] cluster is coordinated by a cysteine rich motif in FliB that is highly conserved among multiple genera of the Enterobacteriaceae family.

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