Abstract
Methyl-coenzyme M reductase, the rate-limiting enzyme in methanogenesis and anaerobic methane oxidation, is responsible for the biological production of more than 1 billion tons of methane per year. The mechanism of methane synthesis is thought to involve either methylnickel(III) or methyl radical/Ni(II)-thiolate intermediates. We employed transient kinetic, spectroscopic, and computational approaches to study the reaction between the active Ni(I) enzyme and substrates. Consistent with the methyl radical-based mechanism, there was no evidence for a methyl-Ni(III) species; furthermore, magnetic circular dichroism spectroscopy identified the Ni(II)-thiolate intermediate. Temperature-dependent transient kinetics also closely matched density functional theory predictions of the methyl radical mechanism. Identifying the key intermediate in methanogenesis provides fundamental insights to develop better catalysts for producing and activating an important fuel and potent greenhouse gas.
| Original language | English |
|---|---|
| Pages (from-to) | 953-958 |
| Number of pages | 6 |
| Journal | Science |
| Volume | 352 |
| Issue number | 6288 |
| DOIs | |
| Publication status | Published - May 20 2016 |
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The radical mechanism of biological methane synthesis by methylcoenzyme M reductase. / Wongnate, Thanyaporn; Sliwa, Dariusz; Ginovska, Bojana; Smith, Dayle; Wolf, Matthew W.; Lehnert, Nicolai; Raugei, Simone; Ragsdale, Stephen W.
In: Science, Vol. 352, No. 6288, 20.05.2016, p. 953-958.Research output: Contribution to journal › Article
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TY - JOUR
T1 - The radical mechanism of biological methane synthesis by methylcoenzyme M reductase
AU - Wongnate, Thanyaporn
AU - Sliwa, Dariusz
AU - Ginovska, Bojana
AU - Smith, Dayle
AU - Wolf, Matthew W.
AU - Lehnert, Nicolai
AU - Raugei, Simone
AU - Ragsdale, Stephen W.
PY - 2016/5/20
Y1 - 2016/5/20
N2 - Methyl-coenzyme M reductase, the rate-limiting enzyme in methanogenesis and anaerobic methane oxidation, is responsible for the biological production of more than 1 billion tons of methane per year. The mechanism of methane synthesis is thought to involve either methylnickel(III) or methyl radical/Ni(II)-thiolate intermediates. We employed transient kinetic, spectroscopic, and computational approaches to study the reaction between the active Ni(I) enzyme and substrates. Consistent with the methyl radical-based mechanism, there was no evidence for a methyl-Ni(III) species; furthermore, magnetic circular dichroism spectroscopy identified the Ni(II)-thiolate intermediate. Temperature-dependent transient kinetics also closely matched density functional theory predictions of the methyl radical mechanism. Identifying the key intermediate in methanogenesis provides fundamental insights to develop better catalysts for producing and activating an important fuel and potent greenhouse gas.
AB - Methyl-coenzyme M reductase, the rate-limiting enzyme in methanogenesis and anaerobic methane oxidation, is responsible for the biological production of more than 1 billion tons of methane per year. The mechanism of methane synthesis is thought to involve either methylnickel(III) or methyl radical/Ni(II)-thiolate intermediates. We employed transient kinetic, spectroscopic, and computational approaches to study the reaction between the active Ni(I) enzyme and substrates. Consistent with the methyl radical-based mechanism, there was no evidence for a methyl-Ni(III) species; furthermore, magnetic circular dichroism spectroscopy identified the Ni(II)-thiolate intermediate. Temperature-dependent transient kinetics also closely matched density functional theory predictions of the methyl radical mechanism. Identifying the key intermediate in methanogenesis provides fundamental insights to develop better catalysts for producing and activating an important fuel and potent greenhouse gas.
UR - http://www.scopus.com/inward/record.url?scp=84971570810&partnerID=8YFLogxK
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U2 - 10.1126/science.aaf0616
DO - 10.1126/science.aaf0616
M3 - Article
VL - 352
SP - 953
EP - 958
JO - Science
JF - Science
SN - 0036-8075
IS - 6288
ER -