Manganese(II) Active Site Mutants of 3,4-Dihydroxyphenylacetate 2,3-Dioxygenase from Arthrobacter globiformis Strain CM-2-Reference-Cited by-同舟云学术

Manganese(II) Active Site Mutants of 3,4-Dihydroxyphenylacetate 2,3-Dioxygenase from Arthrobacter globiformis Strain CM-2

Published:1997-02-01 Issue:8 Volume:36 Page:2147-2153
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Boldt Yvonne R.¹,Whiting Adam K.¹,Wagner Michelle L.¹,Sadowsky Michael J.¹,Que, Lawrence¹,Wackett Lawrence P.¹

Affiliation:

1. Departments of Microbiology and Chemistry and Center for Metals in Biocatalysis, University of Minnesota, Minneapolis, Minnesota 55455, and Departments of Biochemistry and Soil, Water, and Climate and Biological Process Technology Institute and Center for Biodegradation Research and Informatics, University of Minnesota, St. Paul, Minnesota 55108

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi962362i

Reference46 articles.

1. Binding of 17O-labeled substrate and inhibitors to protocatechuate 4,5-dioxygenase-nitrosyl complex. Evidence for direct substrate binding to the active site Fe2+ of extradiol dioxygenases.

2. [17O]Water and nitric oxide binding by protocatechuate 4,5-dioxygenase and catechol 2,3-dioxygenase. Evidence for binding of exogenous ligands to the active site Fe2+ of extradiol dioxygenases.

3. Analysis of three 2,3-dihydroxybiphenyl 1,2-dioxygenases found in Rhodococcus globerulus P6. Identification of a new family of extradiol dioxygenases.

4. The metabolism of cresols by species of Pseudomonas

5. The catabolism of L-tyrosine by an Arthrobacter sp.

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