Structural Basis for Methine Excision by a Heme Oxygenase-like Enzyme-Reference-Cited by-同舟云学术

Structural Basis for Methine Excision by a Heme Oxygenase-like Enzyme

Published:2024-07-24 Issue:8 Volume:10 Page:1524-1536
ISSN:2374-7943
Container-title:ACS Central Science
language:en
Short-container-title:ACS Cent. Sci.

Author:

Simke William C.¹^ORCID,Walker Morgan E.¹^ORCID,Calderone Logan A.²^ORCID,Putz Andrew T.¹,Patteson Jon B.¹^ORCID,Vitro Caitlin N.¹,Zizola Cynthia F.³,Redinbo Matthew R.¹⁴,Pandelia Maria-Eirini²^ORCID,Grove Tyler L.³^ORCID,Li Bo¹^ORCID

Affiliation:

1. Department of Chemistry, The University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, United States

2. Department of Biochemistry, Brandeis University, 415 South Street, Waltham, Massachusetts 02453, United States

3. Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 10461, United States

4. Integrated Program for Biological and Genome Sciences, Department of Biochemistry and Biophysics, and Department of Microbiology, The University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, United States

Funder

Searle Scholars Program

National Institute of Child Health and Human Development

Division of Graduate Education

David and Lucile Packard Foundation

National Institute of General Medical Sciences

Publisher

American Chemical Society (ACS)

Link

https://pubs.acs.org/doi/pdf/10.1021/acscentsci.4c00015

Reference57 articles.

1. Heme Oxygenase: Evolution, Structure, and Mechanism

2. Crystal Structure of Heme Oxygenase from the Gram-Negative Pathogen Neisseria meningitidis and a Comparison with Mammalian Heme Oxygenase-1

3. Crystal Structure of Dimeric Heme Oxygenase-2 from Synechocystis sp. PCC 6803 in Complex with Heme,

4. Quinone biogenesis: Structure and mechanism of PqqC, the final catalyst in the production of pyrroloquinoline quinone