Mitochondrial ATP Synthase Catalytic Mechanism: A Novel Visual Comparative Structural Approach Emphasizes Pivotal Roles for Mg2+ and P-Loop Residues in Making ATP-Reference-Cited by-同舟云学术

Mitochondrial ATP Synthase Catalytic Mechanism: A Novel Visual Comparative Structural Approach Emphasizes Pivotal Roles for Mg2+ and P-Loop Residues in Making ATP

Published:2012-02-09 Issue:7 Volume:51 Page:1532-1546
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Blum David J.¹,Ko Young H.²,Pedersen Peter L.¹

Affiliation:

1. Department of Biological Chemistry, The Johns Hopkins University, School of Medicine, 725 North Wolfe Street, Baltimore, Maryland 21205-2185, United States

2. Cancer Cure Med, LLC, 300 Redland Court, Suite 212, Owings Mills, Maryland 21117, United States

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi201595v

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4. Complete kinetic and thermodynamic characterization of the unisite catalytic pathway of Escherichia coli F1-ATPase. Comparison with mitochondrial F1-ATPase and application to the study of mutant enzymes.

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