Mechanistic Studies of Methane Biogenesis by Methyl-Coenzyme M Reductase:  Evidence that Coenzyme B Participates in Cleaving the C−S Bond of Methyl-Coenzyme M†

Biochemistry ◽  
2001 ◽  
Vol 40 (43) ◽  
pp. 12875-12885 ◽  
Author(s):  
Yih-Chern Horng ◽  
Donald F. Becker ◽  
Stephen W. Ragsdale
Keyword(s):  
Mechanistic Studies ◽  
Coenzyme M ◽  
Coenzyme B ◽  
Methyl Coenzyme M Reductase

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.

Binding of Coenzyme B Induces a Major Conformational Change in the Active Site of Methyl-Coenzyme M Reductase

2010 ◽  
Vol 132 (2) ◽  
pp. 567-575 ◽  
Author(s):  
Sieglinde Ebner ◽  
Bernhard Jaun ◽  
Meike Goenrich ◽  
Rudolf K. Thauer ◽  
Jeffrey Harmer
Keyword(s):  
Conformational Change ◽  
Active Site ◽  
Coenzyme M ◽  
Coenzyme B ◽  
Methyl Coenzyme M Reductase

Coenzyme B Induced Coordination of Coenzyme M via Its Thiol Group to Ni(I) of F430in Active Methyl-Coenzyme M Reductase

2003 ◽  
Vol 125 (17) ◽  
pp. 4988-4989 ◽  
Author(s):  
Cinzia Finazzo ◽  
Jeffrey Harmer ◽  
Carsten Bauer ◽  
Bernhard Jaun ◽  
Evert C. Duin ◽  
...  
Keyword(s):  
Thiol Group ◽  
Coenzyme M ◽  
Active Methyl ◽  
Coenzyme B ◽  
Methyl Coenzyme M Reductase

scholarly journals Structural Insight into Methyl-Coenzyme M Reductase Chemistry Using Coenzyme B Analogues,

Biochemistry ◽  
2010 ◽  
Vol 49 (35) ◽  
pp. 7683-7693 ◽  
Author(s):  
Peder E. Cedervall ◽  
Mishtu Dey ◽  
Arwen R. Pearson ◽  
Stephen W. Ragsdale ◽  
Carrie M. Wilmot
Keyword(s):  
Coenzyme M ◽  
Structural Insight ◽  
Coenzyme B ◽  
Methyl Coenzyme M Reductase ◽  
Insight Into
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