Modulation of Heme Orientation and Binding by a Single Residue in Catalase HPII of Escherichia coli-Reference-Cited by-同舟云学术

Modulation of Heme Orientation and Binding by a Single Residue in Catalase HPII of Escherichia coli

Published:2011-03-03 Issue:12 Volume:50 Page:2101-2110
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Jha Vikash¹,Louis Sherif¹,Chelikani Prashen¹,Carpena Xavi²,Donald Lynda J.¹,Fita Ignacio²,Loewen Peter C.¹

Affiliation:

1. Department of Microbiology, University of Manitoba, Winnipeg, MB R3T 2N2, Canada

2. Institute of Research in Biomedicine (IRB-Barcelona) and Institut de Biología Molecular (IBMB-CSIC), Parc Científic, Baldiri Reixac 10, 08028 Barcelona, Spain

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi200027v

Reference37 articles.

1. The refined structure of beef liver catalase at 2·5 Å resolution

2. Catalase HPII of Escherichia coli catalyzes the conversion of protoheme to cis-heme d

3. Substrate flow in catalases deduced from the crystal structures of active site variants of HPII fromEscherichia coli

4. An Electrical Potential in the Access Channel of Catalases Enhances Catalysis

5. Active and inhibited human catalase structures: ligand and NADPH binding and catalytic mechanism 1 1Edited by R. Huber

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