Design of Heme Enzymes with a Tunable Substrate Binding Pocket Adjacent to an Open Metal Coordination Site-Reference-Cited by-同舟云学术

Design of Heme Enzymes with a Tunable Substrate Binding Pocket Adjacent to an Open Metal Coordination Site

Published:2023-06-21 Issue:26 Volume:145 Page:14307-14315
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Kalvet Indrek¹²³^ORCID,Ortmayer Mary⁴^ORCID,Zhao Jingming⁴^ORCID,Crawshaw Rebecca⁴,Ennist Nathan M.¹²,Levy Colin⁴,Roy Anindya¹²,Green Anthony P.⁴^ORCID,Baker David¹²³

Affiliation:

1. Institute for Protein Design, University of Washington, 3946 W Stevens Way NE, Seattle, Washington 98195, United States

2. Department of Biochemistry, University of Washington, Seattle, Washington 98195, United States

3. Howard Hughes Medical Institute, University of Washington, Seattle, Washington 98195, United States

4. Manchester Institute of Biotechnology, School of Chemistry, 131 Princess Street, The University of Manchester, Manchester M1 7DN, U.K.

Funder

Washington Research Foundation

Advanced Research Projects Agency - Energy

Human Frontier Science Program

H2020 European Research Council

Biotechnology and Biological Sciences Research Council

Open Philanthropy Project

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/jacs.3c02742

Reference58 articles.

1. Cytochrome P450 Compound I: Capture, Characterization, and C-H Bond Activation Kinetics

2. Heme Enzyme Structure and Function

3. Neutron cryo-crystallography captures the protonation state of ferryl heme in a peroxidase

4. The Nature and Reactivity of Ferryl Heme in Compounds I and II

5. Oxygen Activation and Radical Transformations in Heme Proteins and Metalloporphyrins

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