(Q45057874)

9 December 2017

title

Probing the reactivity of Ni in the active site of methyl-coenzyme M reductase with substrate analogues (English)

1 reference

9 December 2017

Meike Goenrich

1

1 reference

9 December 2017

Felix Mahlert

2

1 reference

9 December 2017

Evert C Duin

3

1 reference

9 December 2017

Carsten Bauer

4

1 reference

9 December 2017

Bernhard Jaun

5

1 reference

9 December 2017

Rudolf K Thauer

6

1 reference

9 December 2017

publication date

15 June 2004

1 reference

Journal of Biological Inorganic Chemistry

9 December 2017

published in

1 reference

9 December 2017

volume

9

1 reference

9 December 2017

issue

6

1 reference

9 December 2017

page(s)

691-705

1 reference

https://scigraph.springernature.com/pub.10.1007/s00775-004-0552-1

9 December 2017

exact match

0 references

cites work

Activation of methyl-SCoM reductase to high specific activity after treatment of whole cells with sodium sulfide

1 reference

12 December 2020

On the mechanism of biological methane formation: structural evidence for conformational changes in methyl-coenzyme M reductase upon substrate binding

1 reference

12 December 2020

New insights, ideas and unanswered questions concerning iron-sulfur cluster in mitochondia

1 reference

12 December 2020

Characterization of the MCRred2 form of methyl-coenzyme M reductase: a pulse EPR and ENDOR study

1 reference

12 December 2020

X-ray absorption and resonance Raman studies of methyl-coenzyme M reductase indicating that ligand exchange and macrocycle reduction accompany reductive activation.

1 reference

12 December 2020

Structural modifications and kinetic studies of the substrates involved in the final step of methane formation in Methanobacterium thermoautotrophicum

1 reference

12 December 2020

Theoretical modeling of putative Ni(III)--F(430) intermediates of methylcoenzyme M reductase.

1 reference

12 December 2020

Stable glycyl radical from pyruvate formate-lyase and ribonucleotide reductase (III).

1 reference

12 December 2020

The free radical in pyruvate formate-lyase is located on glycine-734

1 reference

12 December 2020

Methyl-coenzyme M reductase of Methanobacterium thermoautotrophicum delta H catalyzes the reductive dechlorination of 1,2-dichloroethane to ethylene and chloroethane

1 reference

12 December 2020

Coenzyme B induced coordination of coenzyme M via its thiol group to Ni(I) of F430 in active methyl-coenzyme M reductase

1 reference

12 December 2020

The final step in methane formation. Investigations with highly purified methyl-CoM reductase (component C) from Methanobacterium thermoautotrophicum (strain Marburg).

1 reference

12 December 2020

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.

1 reference

12 December 2020

Two genetically distinct methyl-coenzyme M reductases in Methanobacterium thermoautotrophicum strain Marburg and delta H.

1 reference

12 December 2020

Preparation of coenzyme M analogs and their activity in the methyl coenzyme M reductase system of Methanobacterium thermoautotrophicum

1 reference

12 December 2020

Methyl-coenzyme M reductase preparations with high specific activity from H2 -preincubated cells of Methanobacterium thermoautotrophicum

1 reference

12 December 2020

Spectroscopic and computational characterization of the nickel-containing F430 cofactor of methyl-coenzyme M reductase.

1 reference

12 December 2020

Nickel oxidation states of F(430) cofactor in methyl-coenzyme M reductase

1 reference

12 December 2020

Substrate analogues as mechanistic probes of methyl-S-coenzyme M reductase

1 reference

12 December 2020

Biochemistry of methanogenesis: a tribute to Marjory Stephenson. 1998 Marjory Stephenson Prize Lecture

1 reference

12 December 2020

Purified methyl-coenzyme-M reductase is activated when the enzyme-bound coenzyme F430 is reduced to the nickel(I) oxidation state by titanium(III) citrate

1 reference

12 December 2020

Methyl-coenzyme-M reductase from Methanobacterium thermoautotrophicum (strain Marburg). Purity, activity and novel inhibitors

1 reference

12 December 2020

Deconstructing F(430): quantum chemical perspectives of biological methanogenesis

1 reference

12 December 2020

A mechanism from quantum chemical studies for methane formation in methanogenesis

1 reference

12 December 2020

A conspicuous nickel protein in microbial mats that oxidize methane anaerobically

1 reference

12 December 2020

Comparison of three methyl-coenzyme M reductases from phylogenetically distant organisms: unusual amino acid modification, conservation and adaptation

1 reference

12 December 2020

Phylogenetic analysis of 18 thermophilic Methanobacterium isolates supports the proposals to create a new genus, Methanothermobacter gen. nov., and to reclassify several isolates in three species, Methanothermobacter thermautotrophicus comb. nov., M

1 reference

12 December 2020

Properties of the two isoenzymes of methyl-coenzyme M reductase in Methanobacterium thermoautotrophicum

1 reference

12 December 2020

Catalysis by methyl-coenzyme M reductase: a theoretical study for heterodisulfide product formation

1 reference

12 December 2020

Protein Radicals in Enzyme Catalysis

1 reference

12 December 2020

The nickel enzyme methyl-coenzyme M reductase from methanogenic archaea: In vitro induction of the nickel-based MCR-ox EPR signals from MCR-red2.

1 reference

12 December 2020

Methane formation by reaction of a methyl thioether with a photo-excited nickel thiolate--a process mimicking methanogenesis in archaea.

1 reference

12 December 2020

Ethane production by Methanosarcina barkeri during growth in ethanol supplemented medium

1 reference

12 December 2020

The nickel enzyme methyl-coenzyme M reductase from methanogenic archaea: in vitro interconversions among the EPR detectable MCR-red1 and MCR-red2 states

1 reference

12 December 2020

Substrate-analogue-induced changes in the nickel-EPR spectrum of active methyl-coenzyme-M reductase from Methanobacterium thermoautotrophicum

1 reference

12 December 2020

Crystal structure of methyl-coenzyme M reductase: the key enzyme of biological methane formation

1 reference

12 December 2020

Cryoreduction of methyl-coenzyme M reductase: EPR characterization of forms, MCR(ox1) and MCR (red1)

1 reference

12 December 2020

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

1 reference

12 December 2020

Rapid ligand exchange in the MCRred1 form of methyl-coenzyme M reductase

1 reference

12 December 2020

Direct determination of the number of electrons needed to reduce coenzyme F430 pentamethyl ester to the Ni(I) species exhibiting the electron paramagnetic resonance and ultraviolet-visible spectra characteristic for the MCR(red1) state of methyl-coe

1 reference

12 December 2020

Differential expression of the two methyl-coenzyme M reductases in Methanobacterium thermoautotrophicum as determined immunochemically via isoenzyme-specific antisera

1 reference

12 December 2020

The biosynthesis of methylated amino acids in the active site region of methyl-coenzyme M reductase

1 reference

12 December 2020

Methanogenesis: genes, genomes, and who's on first?

1 reference

12 December 2020

10.1007/S00775-004-0552-1

Identifiers

DOI

1 reference

Dimensions Publication ID

9 December 2017

1039017312

0 references

1 reference