(Q73374592)

English

Thermolysis of coenzymes B12 at physiological temperatures: activation parameters for cobalt-carbon bond homolysis and a quantitative analysis of the perturbation of the homolysis equilibrium by the ribonucleoside triphosphate reductase from Lactoba

scientific article published on 01 November 1999

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scholarly article

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3 November 2019

Thermolysis of coenzymes B12 at physiological temperatures: activation parameters for cobalt-carbon bond homolysis and a quantitative analysis of the perturbation of the homolysis equilibrium by the ribonucleoside triphosphate reductase from Lactobacillus leichmannii (English)

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3 November 2019

author name string

K L Brown

1

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3 November 2019

X Zou

2

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3 November 2019

publication date

1 November 1999

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3 November 2019

Journal of Inorganic Biochemistry

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3 November 2019

77

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3 November 2019

3-4

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3 November 2019

185-195

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3 November 2019

A Spectrophotometric Rapid Kinetic Study of Reactions Catalysed by Coenzyme-B12-Dependent Ethanolamine Ammonia-Lyase

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Thermodynamic and kinetic studies on carbon-cobalt bond homolysis by ribonucleoside triphosphate reductase: the importance of entropy in catalysis

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The coenzyme B12 derivative N1-methyl-5'-deoxyadenosylcobalamin: synthesis, characterization, stability towards dimroth rearrangement, and Co-C thermolysis product and kinetic studies

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Coenzyme B(12) Axial-Base Chemical Precedent Studies. Adenosylcobinamide Plus Sterically Hindered Axial-Base Co-C Bond Cleavage Product and Kinetic Studies: Evidence for the Dominance of Axial-Base Transition-State Effects and for Co-N(Axial-Base) D

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Coenzyme B12 and coenzyme B12 model compounds in the catalysis of the dehydration of glycols

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Concerning the mechanism of action of coenzyme B 12 in dioldehydrase and related enzymes. Synthesis and reactions of postulated organocorrin intermediates

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Synthesis and reactions of formylmethylcobalamin and of related compounds

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The acid-catalyzed decomposition of phenacylcobalamin: evidence for the formation of an enol-cobalt(III) π-complex intermediate

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Model for the mechanism of action of coenzyme B12 dependent enzymes. Evidence for .sigma..dbr..pi. rearrangements in cobaloximes

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A direct method for cobalt-carbon bond formation in cobalt(3)-containing cobalamins and cobaloximes. Further support for cobalt(3). Complexes in coenzyme B 12 dependent rearrangements

1 reference

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Letter: Formylmethylcobalamin.

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Letter: On the mechanism of hydrolysis of beta-acetal cobalamins

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Model studies for coenzyme B12 dependent enzyme-catalyzed rearrangements. Kinetics and mechanism of decomposition of formylmethylcobalamin and its acetals

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Water structure in vitamin B12 coenzyme crystals. I. Analysis of the neutron and x-ray solvent densities

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Analysis of cobalamin coenzymes and other corrinoids by high-performance liquid chromatography

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Direct halogenation of sugar moiety of nucleosides

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The Activated Complex in Chemical Reactions

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Solvent Cage Effects in Organocobalt Corrinoid Chemistry: Thermal Homolysis of alpha- and beta-(Cyanomethyl)cobinamides(1)

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On the mechanism of catalysis by vitamin B12.

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7 January 2021

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Alkylcobalamins and alkylcobaloximes. Electronic structure, spectra, and mechanism of photodealkylation

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Coordination of a histidine residue of the protein-component S to the cobalt atom in coenzyme B12-dependent glutamate mutase from Clostridium cochlearium.

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How coenzyme B12 radicals are generated: the crystal structure of methylmalonyl-coenzyme A mutase at 2 A resolution

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Conformational changes on substrate binding to methylmalonyl CoA mutase and new insights into the free radical mechanism

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Stabilization of radical intermediates by an active-site tyrosine residue in methylmalonyl-CoA mutase

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Time-Resolved Spectroscopic Studies of B12Coenzymes: The Photolysis and Geminate Recombination of Adenosylcobalamin

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Thiyl radicals in ribonucleotide reductases.

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Studies on the catalysis of carbon-cobalt bond homolysis by ribonucleoside triphosphate reductase: evidence for concerted carbon-cobalt bond homolysis and thiyl radical formation

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Allosterism, regulation and cooperativity: the case of ribonucleotide reductase of Lactobacillus leichmannii

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Purification and characterization of rabbit haptocorrin.

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Identifiers

10.1016/S0162-0134(99)00190-7

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10643658%20AND%20SRC:MED&resulttype=core&format=json

3 November 2019

PubMed publication ID

1 reference

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3 November 2019

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