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Determinants of Ligand Affinity and Heme Reactivity in H-NOX Domains

Weinert, Emily E. and Plate, Lars and Whited, Charlotte A. and Olea, Charles, Jr. and Marletta, Michael A. (2010) Determinants of Ligand Affinity and Heme Reactivity in H-NOX Domains. Angewandte Chemie International Edition, 49 (4). pp. 720-723. ISSN 1433-7851.

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O_2 balks at extra bulk: The introduction of distal-pocket bulk into the Thermoanaerobacter tengcongensis H-NOX (heme nitric oxide/oxygen) domain caused key changes in the protein structure. Rearrangement of the heme pocket resulted in dramatic differences in O_2-binding kinetics and heme reactivity (see picture).

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Additional Information:© 2010 Wiley. Received: August 27, 2009; revised: October 28, 2009; Published online: December 16, 2009. Funding for this research was provided by the National Institutes of Health National Heart, Lung, and Blood Institute Award F32L090174 (E.E.W.), NIH grant GM 070671 (M.A.M.), and a grant from the Rogers Family Foundation (M.A.M.). We are grateful to Dr. Jay Winkler and the Beckman Institute Laser Resource Center at the California Institute of Technology for assistance with on-rate measurements, and members of the Marletta laboratory for critical reading of this manuscript. H-NOX=heme nitric oxide/oxygen.
Funding AgencyGrant Number
NIHGM 070671
Rogers Family FoundationUNSPECIFIED
Subject Keywords:bioinorganic chemistry; heme proteins; iron; ligand affinity; structural biology
Issue or Number:4
Record Number:CaltechAUTHORS:20100302-131334686
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Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:17629
Deposited By: Jason Perez
Deposited On:08 Mar 2010 21:22
Last Modified:03 Oct 2019 01:30

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