scholarly journals Demonstration That CobG, the Monooxygenase Associated with the Ring Contraction Process of the Aerobic Cobalamin (Vitamin B12) Biosynthetic Pathway, Contains an Fe-S Center and a Mononuclear Non-heme Iron Center

2008 ◽  
Vol 284 (8) ◽  
pp. 4796-4805 ◽  
Author(s):  
Susanne Schroeder ◽  
Andrew D. Lawrence ◽  
Rebekka Biedendieck ◽  
Ruth-Sarah Rose ◽  
Evelyne Deery ◽  
...  
Keyword(s):  
Vitamin B12 ◽  
Biosynthetic Pathway ◽  
Heme Iron ◽  
Ring Contraction ◽  
Non Heme Iron ◽  
Contraction Process ◽  
Iron Center

Aerobic synthesis of vitamin B12: ring contraction and cobalt chelation

2005 ◽  
Vol 33 (4) ◽  
pp. 815-819 ◽  
Author(s):  
D. Heldt ◽  
A.D. Lawrence ◽  
M. Lindenmeyer ◽  
E. Deery ◽  
P. Heathcote ◽  
...  
Keyword(s):  
Vitamin B12 ◽  
Metal Ion ◽  
Biosynthetic Pathway ◽  
Rhodobacter Capsulatus ◽  
Chlorophyll Synthesis ◽  
Subsequent Reduction ◽  
Ring Contraction ◽  
Contraction Process ◽  
Cobalamin Biosynthesis ◽  
Haem Iron

The aerobic biosynthetic pathway for vitamin B12 (cobalamin) biosynthesis is reviewed. Particular attention is focused on the ring contraction process, whereby an integral carbon atom of the tetrapyrrole-derived macrocycle is removed. Previous work had established that this chemically demanding step is facilitated by the action of a mono-oxygenase called CobG, which generates a hydroxy lactone intermediate. This mono-oxygenase contains both a non-haem iron and an Fe-S centre, but little information is known about its mechanism. Recent work has established that in bacteria such as Rhodobacter capsulatus, CobG is substituted by an isofunctional protein called CobZ. This protein has been shown to contain flavin, haem and Fe-S centres. A mechanism is proposed to explain the function of CobZ. Another interesting aspect of the aerobic cobalamin biosynthetic pathway is cobalt insertion, which displays some similarity to the process of magnesium chelation in chlorophyll synthesis. The genetic requirements of cobalt chelation and the subsequent reduction of the metal ion are discussed.

ortho-Hydroxylation of benzoic acids with hydrogen peroxide at a non-heme iron center

2005 ◽  
pp. 5301 ◽  
Author(s):  
Sonia Taktak ◽  
Margaret Flook ◽  
Bruce M. Foxman ◽  
Lawrence Que, Jr. ◽  
Elena V. Rybak-Akimova
Keyword(s):  
Hydrogen Peroxide ◽  
Heme Iron ◽  
Benzoic Acids ◽  
Non Heme Iron ◽  
Iron Center

scholarly journals Computational Study on O-O Bond Formation on a Mononuclear Non-Heme Iron Center

2020 ◽  
Vol 2020 (27) ◽  
pp. 2573-2581
Author(s):  
Chieh-Chih George Yeh ◽  
Gerald Hörner ◽  
Sam P. de Visser
Keyword(s):  
Computational Study ◽  
Bond Formation ◽  
Heme Iron ◽  
Non Heme Iron ◽  
Iron Center

scholarly journals Characterization of the Enzyme CbiH60Involved in Anaerobic Ring Contraction of the Cobalamin (Vitamin B12) Biosynthetic Pathway

2012 ◽  
Vol 288 (1) ◽  
pp. 297-305 ◽  
Author(s):  
Simon J. Moore ◽  
Rebekka Biedendieck ◽  
Andrew D. Lawrence ◽  
Evelyne Deery ◽  
Mark J. Howard ◽  
...  
Keyword(s):  
Vitamin B12 ◽  
Biosynthetic Pathway ◽  
Ring Contraction

Resonance Raman Evidence that Photodissociation of Nitric Oxide from the Non-Heme Iron Center Activates Nitrile Hydratase fromRhodococcussp. N-771†

Biochemistry ◽  
1996 ◽  
Vol 35 (51) ◽  
pp. 16777-16781 ◽  
Author(s):  
Takumi Noguchi ◽  
Mikio Hoshino ◽  
Masanari Tsujimura ◽  
Masafumi Odaka ◽  
Yorinao Inoue ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Nitrile Hydratase ◽  
Resonance Raman ◽  
Heme Iron ◽  
Non Heme Iron ◽  
Iron Center

scholarly journals Highly purified D1/D2/cyt b 559 preparations from spinach do not contain the non-heme iron center

FEBS Letters ◽  
1997 ◽  
Vol 403 (3) ◽  
pp. 283-286 ◽  
Author(s):  
J. Kurreck ◽  
A. Garbers ◽  
F. Parak ◽  
G. Renger
Keyword(s):  
Heme Iron ◽  
Cyt B ◽  
Non Heme Iron ◽  
Iron Center
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