Literature DB >> 168925

A physical explanation of the EPR spectrum observed during catalysis by enzymes utilizing coenzyme B12.

K L Schepler, W R Dunham, R H Sands, J A Fee, R H Abeles.   

Abstract

We have proposed that the "doublet" EPR spectra observed during catalysis by a number of coenzyme B12-requiring enzymes arises from a weak electrostatic exchange interaction between an organic free radical and low spin Co(II), B12r. By varying the magnitude of the exchange of coupling we have quite accurately simulated the published EPR spectra from the enzyme systems: diol dehydrase, glycerol dehydrase, ribonucleotide reductase, and ethanolamine ammon-ia lyase. A dipolar model was shown to be incompatible with the observed properties of these systems.

Entities:  

Mesh：

Substances：

Year:  1975        PMID： 168925     DOI： 10.1016/0005-2744(75)90141-2

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN： 0006-3002


  8 in total

1.  Cobalamin- and corrinoid-dependent enzymes.

Authors:  Rowena G Matthews
Journal:  Met Ions Life Sci       Date:  2009-01-30

2.  Magnetic coupling of the molybdenum and iron-sulphur centres in xanthine oxidase and xanthine dehydrogenases.

Authors:  D J Lowe; R C Bray
Journal:  Biochem J       Date:  1978-03-01       Impact factor: 3.857

3.  EPR and optical changes of the photosystem II reaction center produced by low temperature illumination.

Authors:  H A Frank; O Hansson; P Mathis
Journal:  Photosynth Res       Date:  1989-06       Impact factor: 3.573

4.  The mechanism of cobalamin-dependent rearrangements.

Authors:  J S Krouwer; B M Babior
Journal:  Mol Cell Biochem       Date:  1977-04-12       Impact factor: 3.396

5.  Interaction between the intermediary electron acceptor (pheophytin) and a possible plastoquinone-iron complex in photosystem II reaction centers.

Authors:  V V Klimov; E Dolan; E R Shaw; B Ke
Journal:  Proc Natl Acad Sci U S A       Date:  1980-12       Impact factor: 11.205

6.  Probing interactions from solvent-exchangeable protons and monovalent cations with the 1,2-propanediol-1-yl radical intermediate in the reaction of dioldehydrase.

Authors:  Phillip A Schwartz; Russell Lobrutto; George H Reed; Perry A Frey
Journal:  Protein Sci       Date:  2007-06       Impact factor: 6.725

7.  The synthetic substrate succinyl(carbadethia)-CoA generates cob(II)alamin on adenosylcobalamin-dependent methylmalonyl-CoA mutase.

Authors:  N H Keep; G A Smith; M C Evans; G P Diakun; P F Leadlay
Journal:  Biochem J       Date:  1993-10-15       Impact factor: 3.857

8.  Large-scale domain dynamics and adenosylcobalamin reorientation orchestrate radical catalysis in ornithine 4,5-aminomutase.

Authors:  Kirsten R Wolthers; Colin Levy; Nigel S Scrutton; David Leys
Journal:  J Biol Chem       Date:  2010-01-27       Impact factor: 5.157
  8 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.