scholarly journals Elucidation of the biosynthesis of the methane catalyst coenzyme F430

Nature ◽  
2017 ◽  
Vol 543 (7643) ◽  
pp. 78-82 ◽  
Author(s):  
Simon J. Moore ◽  
Sven T. Sowa ◽  
Christopher Schuchardt ◽  
Evelyne Deery ◽  
Andrew D. Lawrence ◽  
...  
Keyword(s):  
Coenzyme F430

Comparison of chemical properties of iron, cobalt, and nickel porphyrins, corrins, and hydrocorphins

2005 ◽  
Vol 09 (08) ◽  
pp. 581-606 ◽  
Author(s):  
Kasper P. Jensen ◽  
Ulf Ryde
Keyword(s):  
Density Functional ◽  
Hydrolysis Product ◽  
Chemical Properties ◽  
Coenzyme M ◽  
Ring Systems ◽  
Reduction Potentials ◽  
Higher Spin ◽  
Coenzyme F430 ◽  
Coenzyme B ◽  
Methyl Coenzyme M Reductase

Density functional calculations have been used to compare the geometric, electronic, and functional properties of the three important tetrapyrrole systems in biology, heme, coenzyme B 12, and coenzyme F430, formed from iron porphyrin ( Por ), cobalt corrin ( Cor ), and nickel hydrocorphin ( Hcor ). The results show that the flexibility of the ring systems follows the trend Hcor > Cor > Por and that the size of the central cavity follows the trend Cor < Por < Hcor . Therefore, low-spin Co I, Co II, and Co III fit well into the Cor ring, whereas Por seems to be more ideal for the higher spin states of iron, and the cavity in Hcor is tailored for the larger Ni ion, especially in the high-spin Ni II state. This is confirmed by the thermodynamic stabilities of the various combinations of metals and ring systems. Reduction potentials indicate that the +I and +III states are less stable for Ni than for the other metal ions. Moreover, Ni – C bonds are appreciably less stable than Co - C bonds. However, it is still possible that a Ni – CH 3 bond is formed in F 430 by a heterolytic methyl transfer reaction, provided that the donor is appropriate, e.g. if coenzyme M is protonated. This can be facilitated by the adjacent SO 3− group in this coenzyme and by the axial glutamine ligand, which stabilizes the Ni III state. Our results also show that a Ni III– CH 3 complex is readily hydrolysed to form a methane molecule and that the Ni III hydrolysis product can oxidize coenzyme B and M to a heterodisulphide in the reaction mechanism of methyl coenzyme M reductase.

scholarly journals Detection of coenzyme F430 in deep sea sediments: A key molecule for biological methanogenesis

2013 ◽  
Vol 58 ◽  
pp. 137-140 ◽  
Author(s):  
Yoshinori Takano ◽  
Masanori Kaneko ◽  
Jörg Kahnt ◽  
Hiroyuki Imachi ◽  
Seigo Shima ◽  
...  
Keyword(s):  
Deep Sea ◽  
Deep Sea Sediments ◽  
Coenzyme F430

scholarly journals Insights into the Methanogenic Population and Potential in Subsurface Marine Sediments Based on Coenzyme F430 as a Function-Specific Biomarker

JACS Au ◽  
2021 ◽  
Author(s):  
Masanori Kaneko ◽  
Yoshinori Takano ◽  
Masashi Kamo ◽  
Kazuya Morimoto ◽  
Takuro Nunoura ◽  
...  
Keyword(s):  
Marine Sediments ◽  
Coenzyme F430
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