Relationship between Charge-Transfer Interactions, Redox Potentials, and Catalysis for Different Forms of the Flavoprotein Component of p-Cresol Methylhydroxylase-Reference-Cited by-同舟云学术

Relationship between Charge-Transfer Interactions, Redox Potentials, and Catalysis for Different Forms of the Flavoprotein Component of p-Cresol Methylhydroxylase

Published:2004-12-18 Issue:2 Volume:127 Page:732-741
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Efimov Igor¹,McIntire William S.¹

Affiliation:

1. Contribution from the Molecular Biology Division, Department of Veterans Affairs Medical Center, San Francisco, California 94121, and Department of Biochemistry and Biophysics, University of California, San Francisco, California 94143

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja047409z

Reference56 articles.

1. SCNM1, a Putative RNA Splicing Factor That Modifies Disease Severity in Mice

2. Structures of the flavocytochrome p-cresol methylhydroxylase and its enzyme-substrate complex: gated substrate entry and proton relays support the proposed catalytic mechanism

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