Understanding the Mechanism of B12-Dependent Methylmalonyl-CoA Mutase: Partial Proton Transfer in Action-Reference-Cited by-同舟云学术

Understanding the Mechanism of B12-Dependent Methylmalonyl-CoA Mutase: Partial Proton Transfer in Action

Published:1999-09-24 Issue:40 Volume:121 Page:9388-9399
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Smith David M.¹,Golding Bernard T.¹,Radom Leo¹

Affiliation:

1. Contribution from the Research School of Chemistry, Australian National University, Canberra, ACT 0200, Australia, and Department of Chemistry, University of Newcastle upon Tyne, Newcastle upon Tyne NE1 7RU, U.K.

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja991649a

Reference73 articles.

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

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

3. Stabilization of Radical Intermediates by an Active-Site Tyrosine Residue in Methylmalonyl-CoA Mutase,

4. STRUCTURE-BASED PERSPECTIVES ON B12-DEPENDENT ENZYMES

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